ID A0A0G3HGM2_9CORY Unreviewed; 387 AA.
AC A0A0G3HGM2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN Name=apeB {ECO:0000313|EMBL:AKK11088.1};
GN ORFNames=CUTER_05455 {ECO:0000313|EMBL:AKK11088.1};
OS Corynebacterium uterequi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK11088.1, ECO:0000313|Proteomes:UP000035548};
RN [1] {ECO:0000313|EMBL:AKK11088.1, ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|EMBL:AKK11088.1,
RC ECO:0000313|Proteomes:UP000035548};
RX PubMed=26227590;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Virulence Factor Genes Detected in the Complete Genome Sequence of
RT Corynebacterium uterequi DSM 45634, Isolated from the Uterus of a Maiden
RT Mare.";
RL Genome Announc. 3:e00783-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium uterequi DSM 45634, isolated
RT from the uterus of a maiden mare.";
RL Submitted (MAY-2015) 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; CP011546; AKK11088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3HGM2; -.
DR STRING; 1072256.CUTER_05455; -.
DR KEGG; cut:CUTER_05455; -.
DR PATRIC; fig|1072256.5.peg.1078; -.
DR Proteomes; UP000035548; 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 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:UP000035548};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 387 AA; 40790 MW; 45B0E808F2BCAF02 CRC64;
MVASPSAFHA AHEVARHLGF PRQLEQDNFD ASVGGHTIIR GGAVVSYVIP PNPRGVRIIG
AHTDSPGLML KPRPDYQAFG FDQVGVEVYG GPILESFFDR ELTVAGRVVL LDGTEHLVST
GPALRLANLA IHLGREDIDR QAHLSPISLV GPIMEAVAGE LGVEVTDIAG HELITVDAQP
AAITGDVVTS ARLDNLSSVF AGMIALERAA RDVGELDDVV VLAAFNHEEV GSASAQGAAG
SLLEDLLYRL AGALGKDPRQ LIAASSCVSA DAAHSIHPNY PHKHDPQHRP VLGAGPVTKV
NANQRYASDA ATIALWERAS AGIDHQVFVS NNSVRCGSTI GPITATRLGI PTVDVGVPLL
SMHSAREMMS LRDEISLIDA LEAYLTS
//