ID   A0A1I1GJG8_9GAMM        Unreviewed;       435 AA.
AC   A0A1I1GJG8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=SAMN05660443_1480 {ECO:0000313|EMBL:SFC11929.1};
OS   Marinospirillum celere.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinospirillum.
OX   NCBI_TaxID=1122252 {ECO:0000313|EMBL:SFC11929.1, ECO:0000313|Proteomes:UP000199058};
RN   [1] {ECO:0000313|EMBL:SFC11929.1, ECO:0000313|Proteomes:UP000199058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18438 {ECO:0000313|EMBL:SFC11929.1,
RC   ECO:0000313|Proteomes:UP000199058};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOLH01000003; SFC11929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1GJG8; -.
DR   STRING; 1122252.SAMN05660443_1480; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000199058; 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:UP000199058};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   435 AA;  47990 MW;  5D08A8420A658B42 CRC64;
     MQQLDVFNQG LIHFLQASPT PAHAVEVMRR QLQEAGFQEL QEDQDWSLEP GQGYLVIRGG
     KSIVAWRQGL QEPQETGVRM LGAHTDSPCL KVKPKAEIFR NGCLQLGVEV YGGALLHPWF
     DRDLSLAGQV HYLDAQGQIQ EALFDAREPL AIIPSLAIHL NREANKGVEA NPQKHLPVIL
     GQLNVSQNPL FAFRQWLASC LEAEGRQVTE VVDYDLSFYD VQPPAYVGLN KEYLASARLD
     NLLSCYVGME ALIACDQTQD ATSLLICNDH EEVGSASALG AEGPFLESVL RRLTSGNEAS
     YQKLISRSLM ISCDNAHALH PNFADRHDEN HGPKINAGPV IKINANQRYA TSSETSALFD
     AWCRQAQVPC QRFVVRTDMG CGSTIGPLTS TRLGVRVVDV GVPQWAMHSI RETVGSQDPW
     YLARALVAFI QAARV
//