ID C8RWE3_9RHOB Unreviewed; 444 AA.
AC C8RWE3;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:EEW26886.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:EEW26886.1};
GN ORFNames=Rsw2DRAFT_0121 {ECO:0000313|EMBL:EEW26886.1};
OS Rhodobacter sp. SW2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW26886.1, ECO:0000313|Proteomes:UP000010121};
RN [1] {ECO:0000313|EMBL:EEW26886.1, ECO:0000313|Proteomes:UP000010121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW2 {ECO:0000313|EMBL:EEW26886.1,
RC ECO:0000313|Proteomes:UP000010121};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Emerson D.;
RT "The draft genome of Rhodobacter sp. SW2.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:EEW26886.1}.
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DR EMBL; ACYY01000001; EEW26886.1; -; Genomic_DNA.
DR AlphaFoldDB; C8RWE3; -.
DR STRING; 371731.Rsw2DRAFT_0121; -.
DR MEROPS; S41.004; -.
DR eggNOG; COG0793; Bacteria.
DR Proteomes; UP000010121; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:EEW26886.1};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:EEW26886.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010121};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 83..151
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 364..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 47078 MW; 12662A869FBD0DAE CRC64;
MAALGGTVAG ALLTTQVAGP LIAQEATRSA SVYEQLDLFG DIFERIRAQY VEEVQTDKLI
EAAINGMLTS LDPHSSYMAP KDFDDMQVQT RGEFGGLGIE VTQEEGFIKV VSPIDDTPAA
AAGIQSGDFI THVNGESVLG LTLDAAVDKM RGEVGSEIII TVVRKDVADP FDVSIIRDVI
KLTAAKSRVV GNTVVVRLTT FNDQTYPGLV EGIEKSVKEL GGIDKVDGFV LDLRNNPGGL
LTQAIKVSDA FLETGEIVST RGRNPADGER FNATPGDLTG GKPMVVLING GSASASEIVT
GALQDHRRAI VVGTKSFGKG SVQTVIPLRG EGAMRLTTAR YYTPSGRSIQ ALGVSPDIIV
NQPVPPPVAE GTEADTPTSA ANRGRSEADL RGIISNDSMT EDEKRLLEEE RARAEEAAKL
RDEDYQLAYA VDILKGLNAI AAKP
//
