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Database: UniProt
Entry: A0A180EI21_9BACT
LinkDB: A0A180EI21_9BACT
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ID   A0A180EI21_9BACT        Unreviewed;       409 AA.
AC   A0A180EI21;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN   ORFNames=A3850_016855 {ECO:0000313|EMBL:OAV42893.1};
OS   Lewinella sp. 4G2.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC   Lewinella.
OX   NCBI_TaxID=1803372 {ECO:0000313|EMBL:OAV42893.1, ECO:0000313|Proteomes:UP000076582};
RN   [1] {ECO:0000313|EMBL:OAV42893.1, ECO:0000313|Proteomes:UP000076582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G2 {ECO:0000313|EMBL:OAV42893.1,
RC   ECO:0000313|Proteomes:UP000076582};
RA   Wong S.-K., Yoshizawa S., Ogura Y., Tetsuya H., Nakajima Y., Hamasaki K.;
RT   "Lewinella sp. 4G2 Genome sequencing.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OAV42893.1}.
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DR   EMBL; LVWJ02000019; OAV42893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A180EI21; -.
DR   Proteomes; UP000076582; 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   CDD; cd06237; M14_Nna1-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF11; CYTOSOLIC CARBOXYPEPTIDASE 1; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076582};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..409
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008505074"
FT   DOMAIN          163..406
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   409 AA;  46215 MW;  8185C2B8D4E7B7E9 CRC64;
     MRHLAIVLCL CACLLGCNRT ARTYDFPRPV DTNDQPTDIL EGKAWNLGNG ISLSTNFPSA
     RLTEVKVAAP GLITGFVPGE NTPINVSPWY AFLLSSAVDT TLRVQLGYPN TAYHRYWPKL
     SSDGDTWMRI DSTRFRVAPD SKLATLTLRL TAGQPLWVAA QELHDVRRVE TWIEKIARNP
     NVRVESVGTS VGGLSLPKIT IRRPGGSPRR TIVVLSRQHP PEVAGYLAMK AFVEELLADP
     RFSNFIDRYQ VLVYPLLNPD GVELGHWRHN RNGVDLNRDW AFYRQPEIRQ VADDIVRTAR
     KSKAPVVLGL DFHSTWKDVY YTHDDSVQPP SLLGDFKDRW LNTIETEIGG NFKINEEAEP
     IGRPTSMSWF RTQFNAEGIT YEIGDDTPRD FVRRKGQVSA RALITELMK
//
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