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Database: UniProt
Entry: I9NZS5_9ALTE
LinkDB: I9NZS5_9ALTE
Original site: I9NZS5_9ALTE 
ID   I9NZS5_9ALTE            Unreviewed;       468 AA.
AC   I9NZS5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Peptidase M14 carboxypeptidase A {ECO:0000313|EMBL:EIW88122.1};
GN   ORFNames=AGRI_12991 {ECO:0000313|EMBL:EIW88122.1};
OS   Alishewanella agri BL06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alishewanella.
OX   NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW88122.1, ECO:0000313|Proteomes:UP000035062};
RN   [1] {ECO:0000313|EMBL:EIW88122.1, ECO:0000313|Proteomes:UP000035062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL06 {ECO:0000313|EMBL:EIW88122.1,
RC   ECO:0000313|Proteomes:UP000035062};
RX   PubMed=22933763; DOI=10.1128/JB.01129-12;
RA   Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT   "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT   Landfill Soil.";
RL   J. Bacteriol. 194:5135-5136(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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:EIW88122.1}.
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DR   EMBL; AKKU01000025; EIW88122.1; -; Genomic_DNA.
DR   RefSeq; WP_008985386.1; NZ_AKKU01000025.1.
DR   AlphaFoldDB; I9NZS5; -.
DR   STRING; 1195246.AGRI_12991; -.
DR   PATRIC; fig|1195246.3.peg.2579; -.
DR   eggNOG; COG2866; Bacteria.
DR   Proteomes; UP000035062; Unassembled WGS sequence.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:EIW88122.1};
KW   Hydrolase {ECO:0000313|EMBL:EIW88122.1};
KW   Protease {ECO:0000313|EMBL:EIW88122.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035062};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..468
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003722853"
FT   DOMAIN          40..329
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   468 AA;  52632 MW;  3CDB3203D2BA9A98 CRC64;
     MNKFILILLW LGSMMLAQAT TIENYQPYLQ PGLDKARLQL ADIEPLIKQY AADPALKVTE
     LGRSVENRPI YLLQLGQGEK RVMAWSQMHG DEHTATAALF DFLNYTLAPE QQAWREQWFS
     EITLYIVPML NPDGAARNSR VNAQGIDINR DALALQSPEG RLLMQLARRI QPHYGFNLHD
     QNRFHAAGDA PNPATISLLA PAYNAAREIN DSRRRAMQLI AHVKPWLDRQ IPDHLGRYND
     SWSPRSFGDT FAGMGISTVL VEAGGHRNDD NRQVARRLNF QLYVAWINAI VSGSYRDAAL
     SDYEAIPFNN SGGLKDLILS KLQVRVADTE ATLDIGVNFH TEGDRYARIH ELGDLTGYGA
     YHQFDVSGLR YQQGRAYPLT EALLLDDQRY QQLLRLGYTH FSGDAKLLQR QTNLPVLVNP
     LRPTQSSPQL RQGATFLLVN AQGEVIQVLL NGQLLDLARL EVLNPLGT
//
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