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Database: UniProt
Entry: A0A432CFX1_9FLAO
LinkDB: A0A432CFX1_9FLAO
Original site: A0A432CFX1_9FLAO 
ID   A0A432CFX1_9FLAO        Unreviewed;       547 AA.
AC   A0A432CFX1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   SubName: Full=Peptidase M14 {ECO:0000313|EMBL:RTZ01257.1};
GN   ORFNames=EKM02_06915 {ECO:0000313|EMBL:RTZ01257.1};
OS   Flavobacterium sp. RSP49.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2497487 {ECO:0000313|EMBL:RTZ01257.1, ECO:0000313|Proteomes:UP000272024};
RN   [1] {ECO:0000313|EMBL:RTZ01257.1, ECO:0000313|Proteomes:UP000272024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSP49 {ECO:0000313|EMBL:RTZ01257.1,
RC   ECO:0000313|Proteomes:UP000272024};
RA   Liu Q., Xin Y.-H.;
RT   "Flavobacterium sp. nov., isolated from glacier ice.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:RTZ01257.1}.
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DR   EMBL; RYDN01000009; RTZ01257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432CFX1; -.
DR   Proteomes; UP000272024; 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; cd06905; M14-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   PANTHER; PTHR11705:SF145; SLL0236 PROTEIN; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..547
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019448353"
FT   DOMAIN          22..359
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   547 AA;  61201 MW;  F3577E9C23D56FAB CRC64;
     MRKKLLFLFV LCFGITHAQK DYLSYENLTK SLKELDAKSK YCTVKSIGKS SGGREIWVVT
     ISESTTPKPA LLITAGLDGK YRAGTQITLK MIDNVLKNEK LAAILKEKTI YFVPAVNPDA
     IDAAFGAVKM EKRGNDTKTD DDRDGKIGED PFEDLNKDGL ITQLRIEDVT GSFIESPEDS
     RVLIKADPTK NQVGKYVLIS EGIDTDKDGM FNEDFSGGVN IDKNFTFDYP AFEKGAGVYV
     ASEPETRALL DFLYLNQNIY GVLTFGMHNN LSETPKYDSK LASSRIIKGW LEKDSKAAEQ
     VSKLYTQKAA IKGGPKMPMT KGNFAQAAYF HAGRFSFSTP GWWVPKVEAK KDSLYSKLEK
     PAEKDKEELN SEVSFLKWAD SQNIKNVFVD WSVIKHPDFP NQKVEVGGFI PHALNNPPVK
     FLEETANKHV LFVEELLAAM PKIETNVPEV EKIKENLYRV TIKVANKGLL PTYTEIGDKI
     RFVSKMKTEI LLQKNQIMVS GRKYFIRNSM QADESEEYSW LISGTGKVTI TTGCATAGFK
     EVIADLK
//
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