ID   A0A1K1TDQ6_9GAMM        Unreviewed;       440 AA.
AC   A0A1K1TDQ6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=SAMN02745752_00091 {ECO:0000313|EMBL:SFW98783.1};
OS   Marinospirillum alkaliphilum DSM 21637.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinospirillum.
OX   NCBI_TaxID=1122209 {ECO:0000313|EMBL:SFW98783.1, ECO:0000313|Proteomes:UP000182350};
RN   [1] {ECO:0000313|EMBL:SFW98783.1, ECO:0000313|Proteomes:UP000182350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21637 {ECO:0000313|EMBL:SFW98783.1,
RC   ECO:0000313|Proteomes:UP000182350};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FPJW01000001; SFW98783.1; -; Genomic_DNA.
DR   RefSeq; WP_072324358.1; NZ_FPJW01000001.1.
DR   AlphaFoldDB; A0A1K1TDQ6; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000182350; Unassembled WGS sequence.
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:UP000182350};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   440 AA;  47463 MW;  14E587219200F994 CRC64;
     MTQQQAVFNQ GLISFLQASP TPAHAVENMV RQLQEAGFSP LHEGESWVLE PGQGYFLVRG
     GRSLLAFRLG QQPVVEAGVC MMGAHTDSPC LKVKPNPELV RQGYLQLGVE VYGGVLMHPW
     FDRDLSLAGQ VYFRNEAGQL QQALVDLGEP VAVIPSLAIH LNREANKSSE VNAQLHLPPV
     LGAAESAVDG EVAEPALKRL LASWLKREGH QVAEVVDFDL CFYDTQPPAL VGLEQSFISS
     ARLDNLLSCY VGLQALLATD QGQAATSLLV CNDHEEVGSA SAIGAEGPFL ESVLRRLSGD
     EQQYQRMIAR SLLVSCDNAH AVHPNYADKH DENHGPKMNA GPVIKLNANQ RYATSSETAA
     LFAGFCATAG VPVQRFVVRS DMGCGSTIGP IAATRLGVRV VDVGAPQWAM HSIRETAGTQ
     DAWYLCQALQ AFITGWTGQE
//