ID   S5SUH0_9CORY            Unreviewed;       399 AA.
AC   S5SUH0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=B841_06830 {ECO:0000313|EMBL:AGS34839.1};
OS   Corynebacterium maris DSM 45190.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS34839.1, ECO:0000313|Proteomes:UP000015388};
RN   [1] {ECO:0000313|EMBL:AGS34839.1, ECO:0000313|Proteomes:UP000015388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT   45190).";
RL   Submitted (NOV-2012) 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; CP003924; AGS34839.1; -; Genomic_DNA.
DR   RefSeq; WP_020934772.1; NC_021915.1.
DR   AlphaFoldDB; S5SUH0; -.
DR   STRING; 1224163.B841_06830; -.
DR   MEROPS; M18.002; -.
DR   KEGG; cmd:B841_06830; -.
DR   PATRIC; fig|1224163.3.peg.1372; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_11; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000015388; 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:UP000015388};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   399 AA;  42693 MW;  491E34B8D459F397 CRC64;
     MKQTLDLIDF IADSPSSYHA AHVVAQRLEE HGFRRQDETA EWEAAPGGHY LIRGGAVMAW
     WVPEGATAFR IIGSHTDSPG FKLKPQPDFV NQGWQQIATE VYGGPILRSW FDRELTIAGR
     VVLADGSEHL VNTGPVARIP NLAIHLDRDP AVERQTHTQM ITDAPVMEIL AGALGVDAQD
     ICAHDLITAD AQRGAVFGDF LAAGRLDNLT SVHSSLVAFL NAIDSGDATD VLVLAAFDHE
     EVGSQTTTGA GGPILEDVIV RTAQALGHDH RRMIAGSSCV SADAAHAVHP NYAGKHDPTH
     RPLLNHGPVT KVNANQRYAS DATTIALWEQ GSGVPTQSFV SHNDVPCGST IGPITATRLG
     IPTVDVGVPL LSMHSAREMA GVKDLAWFTQ ALEAYLTGY
//