ID C3PG98_CORA7 Unreviewed; 420 AA.
AC C3PG98;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN Name=pepC {ECO:0000313|EMBL:ACP32852.1};
GN OrderedLocusNames=cauri_1259 {ECO:0000313|EMBL:ACP32852.1};
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP32852.1, ECO:0000313|Proteomes:UP000002077};
RN [1] {ECO:0000313|EMBL:ACP32852.1, ECO:0000313|Proteomes:UP000002077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1
RC {ECO:0000313|Proteomes:UP000002077};
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
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; CP001601; ACP32852.1; -; Genomic_DNA.
DR RefSeq; WP_010186640.1; NZ_ACLH01000002.1.
DR AlphaFoldDB; C3PG98; -.
DR STRING; 548476.cauri_1259; -.
DR GeneID; 31923882; -.
DR KEGG; car:cauri_1259; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_11; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000002077; 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 Reference proteome {ECO:0000313|Proteomes:UP000002077};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 420 AA; 44854 MW; 768988094B76C0EE CRC64;
MSTTQDFLDF IAASPSSYHA AEEVARTLVD AGFSRQDESA EWSAAPGGHV MVRGGAVMAW
FVPEGAGPDS GFRIIGSHTD SPGLALKPTP DFDSAGWQQV AVEVYGGVLL HSWFDRELTV
GGQVVLRDGT RHLVNTGPLL RLPSLAIHLY RKDEFKPDRQ RHMQPVLSVG TPETSVMGAV
GKQLGVDPED IASFNLITAD AQRGEVFGAG EKLIAAGRMD NLSSVHASLR ALLAAAKNAD
SIEHKDILVM AAFDHEEVGS SSRYGAGGPI LGDILTRTAR ALGANEEQRF QMFARSSCVS
ADAAHSVHPN YAEKHDPTHH PIIGQGPVTK INGNQRYASD ANTVALWESA CRRADVPVQR
FVGNNDVPCG STIGPISATR LGIPTVDVGV PMLSMHSARE LVGERDQLWL GNALEAYLVG
//
