ID J2WT44_9SPHN Unreviewed; 457 AA.
AC J2WT44;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=PMI04_00591 {ECO:0000313|EMBL:EJK86173.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK86173.1};
RN [1] {ECO:0000313|EMBL:EJK86173.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK86173.1};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJK86173.1}.
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DR EMBL; AJVL01000009; EJK86173.1; -; Genomic_DNA.
DR RefSeq; WP_007705535.1; NZ_CP124576.1.
DR AlphaFoldDB; J2WT44; -.
DR STRING; 1144307.PMI04_00591; -.
DR PATRIC; fig|1144307.3.peg.553; -.
DR eggNOG; COG2234; Bacteria.
DR OrthoDB; 9769665at2; -.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:EJK86173.1};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000313|EMBL:EJK86173.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000313|EMBL:EJK86173.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..457
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003758210"
FT DOMAIN 257..441
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 457 AA; 47441 MW; 47D71212396C03DD CRC64;
MQKIRSGQLA ALLLGSILTP ALAQAAPASD ATIREAALKD DVAWSITEGL TTEVGPRPAA
TPLEARGRDW AVAKLKALGF ANVRAEPYTM PLWERVHDEA AIIAPFPQKL VVAALGNSGS
TPAQGIDGEI AYFPTIADLQ AAPDSAVKGK IVFVSHDMVA AQDGSGYGYY GAARRQGPSI
AAKKGAIAIL VKSIGTDHHR IAHTGVQMWA DGVTPIPAVA VSVPDAEQMA RVVARGKPVR
VHLTAVSKTA KEQPSGNVIA EIPGSDPKAG VIVVACHLDS WDQGTGAIDD ASGCGIVAAA
ALQVANTGTP RRTIRVLFAG AEEVGGNGGR AYFAAHGKEP HALVLESDFG ADKVWKVDFT
LPAGHEALSG RIAQGLAPLG IVPSRDKAHG GSDIEPLVDA GVPVIDLQQD GARYFDIHHT
PDDTLDKVDL TQLRQNVAAW AVTLNIAANA AETLGIN
//
