ID M5BBW7_9MICO Unreviewed; 431 AA.
AC M5BBW7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=CMN_02889 {ECO:0000313|EMBL:CCE76813.1};
OS Clavibacter nebraskensis NCPPB 2581.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=1097677 {ECO:0000313|EMBL:CCE76813.1, ECO:0000313|Proteomes:UP000012170};
RN [1] {ECO:0000313|EMBL:CCE76813.1, ECO:0000313|Proteomes:UP000012170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA Gartemann K.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCE76813.1, ECO:0000313|Proteomes:UP000012170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA Gartemann K.H., Blom J., Dreiseikelmann B., Fluegel M., Jaenicke S.,
RA Linke B., Sczcepanowski R., Wittmann J., Goesmann A., Puehler A.,
RA Eichenlaub R., Rueckert C.;
RT "The genome sequence of the maize-pathogen Clavibacter michiganensis subsp.
RT nebraskensis.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; HE614873; CCE76813.1; -; Genomic_DNA.
DR RefSeq; WP_015491477.1; NC_020891.1.
DR AlphaFoldDB; M5BBW7; -.
DR KEGG; cmc:CMN_02889; -.
DR PATRIC; fig|1097677.3.peg.2439; -.
DR HOGENOM; CLU_019532_2_0_11; -.
DR Proteomes; UP000012170; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 431 AA; 44976 MW; 865B786867EFCF27 CRC64;
MPADRRAHLA DLGRFIQASP SSFHAAEEGA RQLEAAGFAR LDERDAWPTD AGRRFIVRDG
ALLAWIQSAG AHATTPFRVL GTHTDSPGFT LKPKPTIGSD GWVQAGVEVY GGPLLNSWLD
RDLELAGRLV TRDGRRHLVR TGPLLRFPQL AVHLDRGVNT DGLRLDPQRY MSPILGTGSP
ADADVLGHLA GLAGVAADDV LGYDVGVADT QAPGSLGFDG ELFAAGRMDN LSSVHAGLAA
LLELAATADD DPEAPIAVLA AFDHEEVGSA TASGAAGPIL EDVLGRISAG LGASSEERRR
AFASSWCLSA DAGHAVHPNY PDRHDPANRP VPNGGPLLKI NANQRYATDG VGAREWALAC
ERAGVPFQEF VSSNAVPCGS TIGPITATRL GIRTVDVGIP LLSMHSAREL CGADDPGHLA
AAAAAFLRPA A
//
