ID A0A0Q4FPS2_9SPHN Unreviewed; 540 AA.
AC A0A0Q4FPS2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=ASE75_01105 {ECO:0000313|EMBL:KQM67567.1};
OS Sphingomonas sp. Leaf17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM67567.1, ECO:0000313|Proteomes:UP000051777};
RN [1] {ECO:0000313|EMBL:KQM67567.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM67567.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM67567.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM67567.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KQM67567.1}.
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DR EMBL; LMKL01000001; KQM67567.1; -; Genomic_DNA.
DR RefSeq; WP_055927559.1; NZ_LMKL01000001.1.
DR AlphaFoldDB; A0A0Q4FPS2; -.
DR STRING; 1735683.ASE75_01105; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000051777; 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; 2.
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:UP000051777};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..540
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006217777"
FT DOMAIN 288..505
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 519..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 58122 MW; E4D0E96DAF29F376 CRC64;
MRHLFLAATA TLAVVSAAMP ATAQDKPASP VLNRIIDEGT NRTQVMTTAQ HLTDVIGPRL
TNSPAMRRAE AWTQEEFRRY GLVNVHKEAF PFGRGWSIER SSVRMVTPRV VQLTAIPIAW
TPATTGALTA PVIVAPIDKE RDFAKWRGKL SGKIVMLSAP GTGDEPTDPA FRRLAGDDIA
KLDVFQQPSY DPAAADRRLK RLDFAQKLDA FLKAEGAVGF ATISYRDGKL VSGEGYQFGV
GETPSMPGVQ IAAEDYRRLA RLSVSGPAPT LEIISDVRFD DSDTNAYNII AEIPGTDPKA
GYVMAGAHLD SWVAADGAAD NAAGSAMIME AARILAATGV RPKRAIRFAL WSGEEQGILG
SMAYVEQHLA RRGSPGDPKQ SGMKSYYGFA NRWPITPLPG HGDLAAYFNI DNGSGKLRGL
YAENNPSVVP IFREWLGPLA SMGAGNVVAR QTGGTDHVFM QSVGIPGFQF IQDPLDYGSR
IHHTSADTFD HLKATDMRQA SIVLASVLLS AANADKALPR PPVPTKPVVT DPFAISEDDD
//
