ID A0A1L6R3F1_9FLAO Unreviewed; 472 AA.
AC A0A1L6R3F1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=AO058_09150 {ECO:0000313|EMBL:APS39025.1};
OS Salegentibacter sp. T436.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salegentibacter.
OX NCBI_TaxID=1729720 {ECO:0000313|EMBL:APS39025.1, ECO:0000313|Proteomes:UP000185442};
RN [1] {ECO:0000313|EMBL:APS39025.1, ECO:0000313|Proteomes:UP000185442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T436 {ECO:0000313|EMBL:APS39025.1,
RC ECO:0000313|Proteomes:UP000185442};
RA Spain J.C., Graham D.E., Mahan K.M., Klingeman D.M., Giannone R.J.,
RA Hettich R.L., Parry R.J.;
RT "Complete genome sequence of Salegentibacter sp. T436.";
RL Submitted (OCT-2015) 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}.
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DR EMBL; CP012872; APS39025.1; -; Genomic_DNA.
DR RefSeq; WP_075326172.1; NZ_CP012872.1.
DR AlphaFoldDB; A0A1L6R3F1; -.
DR STRING; 1729720.AO058_09150; -.
DR KEGG; salt:AO058_09150; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000185442; Chromosome.
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; IPR003137; PA_domain.
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; PF02225; PA; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..472
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013086384"
FT DOMAIN 145..235
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 264..448
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 472 AA; 52304 MW; 39B24E7581452D60 CRC64;
MKLYIFAFFG LFLTLNLNAQ APETKEDSLK IREIYSAALV NGKAYNWLDH LSNKIGGRLS
GSLNAQKAVE YTKTQLEELG LDKVWLQPVM VPKWTRGARE HAYIQTGPGM TTEVSITALG
GSVATATGGL KANVIEVQGI EDLENYKDEI KGKIVFYNRP MNPELIQTFE AYGGCVDQRY
SGAEAAAKYG AAGVIVRSLS HKIDENPHTG SMSYGDLPNN KRIPAAAIST KDAEYLSGIL
KLKKDLEFYF KLSSENHGEV QSYNVIGEIT GSEFPEEIMV VGGHLDSWDL GDGSHDDGAG
VVQSMEVLRL FKETVYKPKR TIRVVLFMNE ENGLRGGNKY ADVAHSKNEN HIFALESDAG
GFTPRGFSFE ADDAQFAQIE SWKPLFEPYL IHYFEKGGSG ADIGPLKKGD IVLAGLRPDS
QRYFDHHHAA TDTFEHVNKR ELELGAATMT SLIYLVDKYG IKRINLEKDQ KL
//
