ID A3XFG1_9RHOB Unreviewed; 451 AA.
AC A3XFG1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Carboxyl-terminal protease family protein {ECO:0000313|EMBL:EAQ43444.1};
GN ORFNames=MED193_11679 {ECO:0000313|EMBL:EAQ43444.1};
OS Roseobacter sp. MED193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ43444.1, ECO:0000313|Proteomes:UP000005943};
RN [1] {ECO:0000313|EMBL:EAQ43444.1, ECO:0000313|Proteomes:UP000005943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ43444.1,
RC ECO:0000313|Proteomes:UP000005943};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ43444.1}.
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DR EMBL; AANB01000017; EAQ43444.1; -; Genomic_DNA.
DR AlphaFoldDB; A3XFG1; -.
DR STRING; 314262.MED193_11679; -.
DR MEROPS; S41.004; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_1_1_5; -.
DR Proteomes; UP000005943; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:EAQ43444.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 93..161
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 372..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48392 MW; AAEA4099E205BC15 CRC64;
MDEGFMRKFA MAAIGGTLAG IVATTYVAGP LLAQEANREA TVYEQLDLFG DIFERIRAQY
VEEVDEKELI EAAIGGMLTS LDPHSSYLKP DDAASMQVQT RGEFGGLGIE VTQEEGFVKV
VSPIDGTPAD EAGMEAGDFI THVDGESVLG LGLDEAVDLM RGPVGSEIVI TVVREGEGEP
FDVSIIRDTI KLTAVRARTE GETVVLRITT FNRQTTPNLE SGLKEQIEEA GGIDKVSGIV
LDLRNNPGGL LTEAISVADS FLDSGEIVST RGRNPEDGER FNATPGDLSD GKPIVVLING
GSASASEIVA GALQDHRRAI VVGTKSFGKG SVQTVMPLRG NGAMRLTTAR YYTPSGRSIQ
ALGVSPDIVV EQPRRTPETE EAEEESAARR TRTEADLRGS LNNDSLTEDE IRQIKEDRER
AEKAAALREQ DYQLAYAIDI LKGLVALGPK Q
//
