data_FAM_000077
#
_pdbx_reference_molecule_family.family_prd_id   FAM_000077
_pdbx_reference_molecule_family.name            Microcin
_pdbx_reference_molecule_family.release_status  REL
_pdbx_reference_molecule_family.replaces        ?
_pdbx_reference_molecule_family.replaced_by     ?
#
loop_
_pdbx_reference_molecule_list.family_prd_id
_pdbx_reference_molecule_list.prd_id
FAM_000077   PRD_000183  
FAM_000077   PRD_000184  
FAM_000077   PRD_001126  
FAM_000077   PRD_001129  
#
loop_
_pdbx_reference_molecule_synonyms.family_prd_id
_pdbx_reference_molecule_synonyms.prd_id
_pdbx_reference_molecule_synonyms.ordinal
_pdbx_reference_molecule_synonyms.source
_pdbx_reference_molecule_synonyms.name
FAM_000077   PRD_000183   1     PDB          "Microcin C7"
FAM_000077   PRD_000183   2     PDB          MccC7
FAM_000077   PRD_000183   3     PDB          "Microcin C51"
FAM_000077   PRD_000183   4     PDB          McC
FAM_000077   PRD_000183   5     PDB          MccC51
FAM_000077   PRD_000183   6     PDB          "Microcin C"
FAM_000077   PRD_000184   7     PDB          "Microcin J25"
FAM_000077   PRD_001126   8     PDB          SeMet-MccA
FAM_000077   PRD_001129   9     PDB          MccA-N7isoASN
#
loop_
_pdbx_reference_molecule_annotation.family_prd_id
_pdbx_reference_molecule_annotation.prd_id
_pdbx_reference_molecule_annotation.ordinal
_pdbx_reference_molecule_annotation.source
_pdbx_reference_molecule_annotation.type
_pdbx_reference_molecule_annotation.text
FAM_000077   PRD_000183   1     Bactibase            "Mechanism of action"     "Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp."
FAM_000077   PRD_000183   2     Bactibase            Structure
;Post-translational modification: The peptide moiety allows entry into the bacterial cell, where it undergoes proteolytic cleavage to release the aspartyl adenylate analog, which is responsible for aspartyl-tRNA synthetase inhibition. Can be processed by the non-specificoligopeptidases pepA, pepB and pepN.
;
FAM_000077   PRD_000184   3     Bactibase            "Mechanism of Action"     "Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). May inhibit transcription by binding in RNAP secondary channel and blocking nucleotide substrates access to the catalytic center. Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. Induces bacterial filamentation in susceptible cells in a non-SOS-dependent way, but this phenotype may result from impaired transcription of genes coding for cell division proteins."
FAM_000077   PRD_001126   4     PMID:19494832        Function                  "Substrate of MccB"
FAM_000077   PRD_001129   5     PMID:19494832        Function                  "Reaction intermediate of MccB"
#
loop_
_pdbx_reference_molecule_features.family_prd_id
_pdbx_reference_molecule_features.prd_id
_pdbx_reference_molecule_features.ordinal
_pdbx_reference_molecule_features.source_ordinal
_pdbx_reference_molecule_features.source
_pdbx_reference_molecule_features.type
_pdbx_reference_molecule_features.value
FAM_000077   PRD_000183   1     1     UniProt                External_Reference_ID     Q47505
FAM_000077   PRD_000184   2     1     UniProt                External_Reference_ID     Q9X2V7
FAM_000077   PRD_000183   3     1     Bactibase              External_Reference_ID     BAC207
FAM_000077   PRD_000184   4     1     Bactibase              External_Reference_ID     BAC015
#
loop_
_citation.id
_citation.year
_citation.journal_volume
_citation.page_first
_citation.page_last
_citation.pdbx_database_id_DOI
_citation.pdbx_database_id_PubMed
_citation.title
_citation.journal_abbrev
 1  2002   99   2696   2701  10.1073/pnas.052709699                ?  " Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae, induces apoptosis in some human cell lines"                  Proc.Nat.Acad.Sci.(USA)  
 2  2008  275   4088   4096  ?                              18616579  " Microcin J25 induces the opening of the mitochondrial transition pore and cytochrome c release through superoxide generation."        "FEBS J."  
 3  1996  274   1188   1193  10.1126/science.274.5290.1188         ?  " From Peptide Precursors to Oxazole and Thiazole-Containing Peptide Antibiotics: Microcin B17 Synthase"                                Science  
 4  2003  125  12464  12474  10.1021/ja0367703                     ?  " Microcin J25 Has a Threaded Sidechain-to-Backbone Ring Structure and Not a Head-to-Tail Cyclized Backbone"                            "J. Am. Chem. Soc.,"  
 5  2009   10     74     85  10.2174/138920109787048643            ?  " Antibacterial and Antitumorigenic Properties of Microcin E492, a Pore-Forming Bacteriocin"                                            "Current Pharmaceutical Biotechnology"  
 6  2005  285    118    124  10.1016/j.jcis.2004.11.025            ?  " Penetration and interactions of the antimicrobial peptide, microcin J25, into uncharged phospholipid monolayers"                      "Journal of Colloid and Interface Science"  
 7  2001  307   1223   1234  10.1006/jmbi.2001.4562                ?  " The Antibiotic Microcin B17 is a DNA Gyrase Poison: Characterisation of the Mode of Inhibition"                                       "J. Mol. Biol."  
 8  1992  174   7428   7435  ?                                207439  "Microcin 25, a novel antimicrobial peptide produced by Escherichia coli."                                                              "J Bacteriol."  
 9  2002   84    521    529  ?                              12423796  "The regulation of microcin B, C and J operons"                                                                                         Biochimie  
10  1999    6    305    318  ?                              10322125  " In vivo processing and antibiotic activity of microcin B17 analogs with varying ring content and altered bisheterocyclic sites"       "Chemistry & Biology"  
11  1995  357    235    238  10.1016/0014-5793(94)01345-2          ?  "Structure of microcin C51, a new antibiotic with a broad spectrum of activity"                                                         "FEBS Letters"  
12  1995  270  23520  23532  10.1074/jbc.270.40.23520              ?  "Chemical Structure and Translation Inhibition Studies of the Antibiotic Microcin C7"                                                   "The Journal of Biological Chemistry"  
13  1982   36    325    327  ?                               6339460  "Microcin 15N: a second antibiotic from escherichia coli lp15"                                                                          "The Journal of Antibiotics"  
14  2003  125  12475  12483  ?                              14531691  "Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail "                                        "J. Am. Chem. Soc."  
15  2003  125  12382  12383  ?                              14531661  "Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot"                                                        "J. Am. Chem. Soc."  
16  2004   14    753    762  ?                              15200953  "Molecular mechanism of transcription inhibition by peptide antibiotic microcin J25"                                                    "Mol. Cell"  
17  2001   45    969    972  10.1128/AAC.45.3.969-972.2001         ?  " The Structure, Function, and Origin of the Microcin H47 ATP-Binding Cassette Exporter Indicate Its Relatedness to That of Colicin V"  "Antimicrobial Agents and Chemotherapy"  
18  1994   91   4519   4523  ?                               8183941  "Posttranslational Modifications in Microcin B17 Define an Additional Class of DNA Gyrase Inhibitor"                                    "Proc Natl Acad Sci U S A."  
#
loop_
_citation_author.citation_id
_citation_author.ordinal
_citation_author.name
 1    1  "Hetz, C."  
 1    2  "Bono, M.R."  
 1    3  "Barros, L.F."  
 1    4  "Lagos, R."  
 2    5  "Niklison, C.M."  
 2    6  "Bellomio, A."  
 2    7  "Dupuy, F."  
 2    8  "Arcuri, B."  
 2    9  "Minahk, C."  
 2   10  "Morero, R."  
 3   11  "Li, Y.-M."  
 3   12  "Milne, J.C."  
 3   13  "Madison, L.L."  
 3   14  "Kolter, R."  
 3   15  "Walsh, C.T."  
 4   16  "Rosengren, K.J."  
 4   17  "Clark, R.J."  
 4   18  "Daly, N.L."  
 4   19  "Goransson, U."  
 4   20  "Jones, A."  
 4   21  "Craik, D.J."  
 5   22  "Lagos, R."  
 5   23  "Tello, M."  
 5   24  "Mercado, G."  
 5   25  "Garcia, V."  
 5   26  "Monasterio, O."  
 6   27  "Bellomio, A."  
 6   28  "Oliveira, R.G."  
 6   29  "Maggio, B."  
 6   30  "Morero, R.D."  
 7   31  "Heddle, J.G."  
 7   32  "Blance, S.J."  
 7   33  "Zamble, D.B."  
 7   34  "Hollfelder, F."  
 7   35  "Miller, D.A."  
 7   36  "Wentzell, L.M."  
 7   37  "Walsh, C.T."  
 7   38  "Maxwell, A."  
 8   39  "Salomon, R.A."  
 8   40  "Farias, R.N."  
 9   41  "Moreno, F."  
 9   42  "Gonzalez-Pastor, J.E."  
 9   43  "Baquero, M.-R."  
 9   44  "Bravo, D."  
10   45  "Roy, R.S."  
10   46  "Kelleher, N.L."  
10   47  "Milne, J.C."  
10   48  "Walsh, C.T."  
11   49  "Metlitskaya, A.Z."  
11   50  "Katrukha, G.S."  
11   51  "Shashkov, A.S."  
11   52  "Zaitsev, D.A."  
11   53  "Egorov, Ts.A."  
11   54  "Khmel, I.A."  
12   55  "Guijarro, J.I."  
12   56  "Gonzalez-Pastor, J.E."  
12   57  "Baleux, F."  
12   58  "San Mill, J.L."  
12   59  "Castilla, M.A."  
12   60  "Rico, M."  
12   61  "Moreno, F."  
12   62  "Delepierre, M."  
13   63  "Aguilar, A."  
13   64  "Baquero, F."  
13   65  "Martinez, J.L."  
13   66  "Asensio, C."  
14   67  "Wilson, K.-A."  
14   68  "Kalkum, M."  
14   69  "Ottesen, J."  
14   70  "Yuzenkova, J."  
14   71  "Chait, B.T."  
14   72  "Landick, R."  
14   73  "Muir, T."  
14   74  "Severinov, K."  
14   75  "Darst, S.A."  
15   76  "Bayro, M.J."  
15   77  "Mukhopadhyay, J."  
15   78  "Swapna, G.V.T."  
15   79  "Huang, J.Y."  
15   80  "Ma, L.-C."  
15   81  "Sineva, E."  
15   82  "Dawson, P.E."  
15   83  "Montelione, G.T."  
15   84  "Ebright, R.H."  
16   85  "Adelman, K."  
16   86  "Yuzenkova, J."  
16   87  "La Porta, A."  
16   88  "Zenkin, N."  
16   89  "Lee, J."  
16   90  "Lis, J.T."  
16   91  "Borukhov, S."  
16   92  "Wang, M.D."  
16   93  "Severinov, K."  
17   94  "Azpiroz, M.F."  
17   95  "Rodriguez, E."  
17   96  "Lavina, M."  
18   97  "Yorgey, P."  
18   98  "Lee, J."  
18   99  "Kordel, J."  
18  100  "Vivas, E."  
18  101  "Warner, P."  
18  102  "Jebaratnam, D."  
18  103  "Kolter, R."  
#
loop_
_pdbx_family_prd_audit.family_prd_id
_pdbx_family_prd_audit.date
_pdbx_family_prd_audit.processing_site
_pdbx_family_prd_audit.action_type
FAM_000077	2012-02-08	RCSB	"Create family"	
FAM_000077	2013-10-16	RCSB	"Initial release"	
#
