ID   A0A1I5SHP1_9BACT        Unreviewed;       828 AA.
AC   A0A1I5SHP1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:SFP70280.1};
GN   ORFNames=SAMN05444277_101771 {ECO:0000313|EMBL:SFP70280.1};
OS   Parafilimonas terrae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Parafilimonas.
OX   NCBI_TaxID=1465490 {ECO:0000313|EMBL:SFP70280.1, ECO:0000313|Proteomes:UP000199031};
RN   [1] {ECO:0000313|EMBL:SFP70280.1, ECO:0000313|Proteomes:UP000199031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28286 {ECO:0000313|EMBL:SFP70280.1,
RC   ECO:0000313|Proteomes:UP000199031};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOXQ01000001; SFP70280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5SHP1; -.
DR   STRING; 1465490.SAMN05444277_101771; -.
DR   OrthoDB; 9758209at2; -.
DR   Proteomes; UP000199031; 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; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   CDD; cd06238; M14-like; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
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; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SFP70280.1};
KW   Hydrolase {ECO:0000313|EMBL:SFP70280.1};
KW   Protease {ECO:0000313|EMBL:SFP70280.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199031};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..828
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011453652"
FT   DOMAIN          37..311
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   828 AA;  92789 MW;  7B62DEFC7B1AF568 CRC64;
     MKRINIITIL LCITTILSAQ NIPSPKQFLG YELGERFTPC YKIDNYFNAV AQASPSTVKT
     FKYGETNEGR DLIVAFISSA QNIQNLENIR QNNLRLAGML KDNTPADVNA PTIVWLSYNV
     HGNEPSSSEA AMKVLYALAD ASNTQTKQWL QNVVVIIDPI QNPDGRDRYI NWYNNAVGKN
     FNADPQSREH DEPWPYGRTN HYNFDLNRDW AWQTQKETQQ KMKLYNQWLP QIHVDLHEQG
     YNAPYYFAPA AQPFHEVVTQ WQRDFQVTVG KNNAKYFDAN GWLYFTKQIF DLFYPSYGDT
     YPTYNGAIGM TYEQGGIGAG LGIKTRSGDT LTLTDRLMHH YTSSISTIEV ASNNAKQLVT
     EYKKYFDNNV NGVDLGNTTY VLTSSDQNKI EAVRKLLDNN GISYGATNTS FSGYNYIDNK
     TEVFKNEGYQ IAVNTLQPKG RMVKVLFERE SKLVDSATYD ITAWSIPYVY GVNAWATKDK
     ISLSAYTMPA AVTPVQSNYG VLIPYTSINA SKVLAALLSQ GIRVRYSADD FTYNGKAFNK
     GTLIILKGNN QPTWLNAVNT ACSSYNVQPF AVETGFMDAG ADFGSSDVHF IKAPRVALLT
     GKNVSYIASG EVWSYFDNEL NYPISQLMAE DMDDINLSNY DVLIMPDGGY DVFDDKTNAA
     KLEDFVKGGG KLIATESGAE KLADFNWSGL KLIEDTAQSS DSIVQKNYGA SERDFLTSFI
     PGAIYKLQLD NTHPIAYGYP NFYYTLKQDA RVYESVKGGW NVGIFPSNAY VAGFVGSTLK
     SKLKQGVAIG EKRYGKGNII FFNDDVLFRQ FWQNGKMLFA NAVFLAGN
//