ID   A0A147END4_9MICO        Unreviewed;       452 AA.
AC   A0A147END4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=NS354_07040 {ECO:0000313|EMBL:KTR85951.1};
OS   Leucobacter chromiiresistens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR85951.1, ECO:0000313|Proteomes:UP000070810};
RN   [1] {ECO:0000313|EMBL:KTR85951.1, ECO:0000313|Proteomes:UP000070810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS354 {ECO:0000313|EMBL:KTR85951.1,
RC   ECO:0000313|Proteomes:UP000070810};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTR85951.1}.
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DR   EMBL; LDRK01000034; KTR85951.1; -; Genomic_DNA.
DR   RefSeq; WP_058593862.1; NZ_LDRK01000034.1.
DR   AlphaFoldDB; A0A147END4; -.
DR   PATRIC; fig|1079994.3.peg.1529; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000070810; 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:UP000070810};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   452 AA;  47480 MW;  98A28F62CE801E20 CRC64;
     MTPVSRSQLH DRDAYISAFG DFVSASPSSY HAAGAVCETL SKAGFAEHDE TAAWSPLEAS
     GRGFVRRDGA VIAWRAGAEV DATSPVRVLG AHTDSPGFVV KPRPDFESDG WAQVGVEIYG
     GPLLTSWLDR DLGFAGRIVT RDGAEHLVRT GAVARIPQLA IHLDRDANKS LTLDRQRHTQ
     PVIGLAGEEL SVLALLVREL GGGRTGSGRG RAAARSAARA ALTPEDLAGI DVRLYDTQAP
     QRIGANGELF ASPRLDNLSS TYAGLAALLD TEPHPGTISM IAAFDHEELG SNTRSGAAGP
     FLSDVLDRLR AGLGASGEDA ARALAGSWCL SADAGHSVHP NYSEKHDPRV RPLAGRGPML
     KINANQRYAS DAHGAALWSR LGSAAEVPTQ EFVSNNTVPC GSTIGPITAT RLGIRTVDVG
     VPLLSMHSAR ELAHVDDLFG LAKITGAFFA TA
//