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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//