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Database: UniProt
Entry: A0A257LF54_9BACT
LinkDB: A0A257LF54_9BACT
Original site: A0A257LF54_9BACT 
ID   A0A257LF54_9BACT        Unreviewed;       456 AA.
AC   A0A257LF54;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=CFE21_04690 {ECO:0000313|EMBL:OYU97595.1};
OS   Bacteroidetes bacterium B1(2017).
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=2015582 {ECO:0000313|EMBL:OYU97595.1, ECO:0000313|Proteomes:UP000216329};
RN   [1] {ECO:0000313|EMBL:OYU97595.1, ECO:0000313|Proteomes:UP000216329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|EMBL:OYU97595.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homodimer. The monomeric form is inactive while the homodimer
CC       is active. {ECO:0000256|ARBA:ARBA00025833}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC       {ECO:0000256|ARBA:ARBA00004555}. Lysosome
CC       {ECO:0000256|ARBA:ARBA00004371}.
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:OYU97595.1}.
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DR   EMBL; NKJG01000001; OYU97595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257LF54; -.
DR   Proteomes; UP000216329; Unassembled WGS sequence.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR039866; CPQ.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12053:SF3; CARBOXYPEPTIDASE Q; 1.
DR   PANTHER; PTHR12053; PROTEASE FAMILY M28 PLASMA GLUTAMATE CARBOXYPEPTIDASE-RELATED; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000256|ARBA:ARBA00022645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216329};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..456
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013373472"
FT   DOMAIN          259..447
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   456 AA;  49549 MW;  820726AA77303B3A CRC64;
     MKNKILFLIG LMAFLPNLLI AQSDSLQVRK IVNQILLDGQ CYKRLDYLSN SIGGRLSGSK
     EAEAAVNYTF DILKKEGFDS VWLQPVLVPH WVRGQKEEAW YWVGKKKIIP TICALGGSCG
     TDKKGLEAEV IEVKSIKELQ ALGSEKIKGK IVFYNRPMNP LFIKTFEAYG DAVDQRAAGA
     VEASKLGAVG VIVRSMGSNI DKHPHTGVMR VLPEVKQIPA CAISTFDAEE LSLALKANSR
     LTFSFKMSCA TLADVWSYNV VAQINGSEKA DEIIVVGGHL DSWDNGDGAH DDGAGVVQSM
     EVLHTYKALG LKPKRSIRCV LFMNEENGAK GASAYAAFAK QNQEKHIAAI ESDAGGFTPR
     NFGATTDDAK LAKLRTWAPL LKQYGIEEVL SSGGGVDIGP LKEQGCTLIG FGPDSQRYFD
     VHHTAVDTFD KVSKRELELG AANIAALVWL ISENGL
//
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