ID G4RH07_PELHB Unreviewed; 468 AA.
AC G4RH07;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:AEQ53160.1};
GN OrderedLocusNames=KKY_3171 {ECO:0000313|EMBL:AEQ53160.1};
OS Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS B2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Devosiaceae; Pelagibacterium.
OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ53160.1, ECO:0000313|Proteomes:UP000008850};
RN [1] {ECO:0000313|EMBL:AEQ53160.1, ECO:0000313|Proteomes:UP000008850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC {ECO:0000313|Proteomes:UP000008850};
RX PubMed=22156395; DOI=10.1128/JB.06343-11;
RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL J. Bacteriol. 194:197-198(2012).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP003075; AEQ53160.1; -; Genomic_DNA.
DR AlphaFoldDB; G4RH07; -.
DR STRING; 1082931.KKY_3171; -.
DR MEROPS; S41.004; -.
DR KEGG; phl:KKY_3171; -.
DR PATRIC; fig|1082931.4.peg.3124; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_1_2_5; -.
DR Proteomes; UP000008850; Chromosome.
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:AEQ53160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008850};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 101..169
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 441..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 50409 MW; 46654AF126A94FA1 CRC64;
MVDGPVPTTG KWNELMALVF KRVLIVMLAI AASMGPVSAQ DQTQLEQEEL YRQLELFGLV
LDRIRDEYIE APDETELIRA AIQGMLTSLD PHSAYLSPES FADVREDTSG TFGGLGIEVT
MEEGLVKVVT PYDDSPASRA GILANDYVVE IDGQQVMGMT LDDAVELMRG EVGTDVEIVI
SREGAEQLIE LTLTRDIISV AAVRWNMERE VPLIRLSRFS GQAYSGLSDA IQEIFEENDG
EAPQGIILDL RNNPGGLVDQ AQFVADAFLS QGSVVLTRGR IPNQNSRYDA SPDEIDAMLT
DVPVIVLING GSASAAEIVA GALQDQGRAT LVGTRSFGKG SVQSIIPLGF DGAMRLTTAR
YYTPNNRSIQ ALGITPDIEV LQDVPEEFQG RDLLIGEAGL AGHISGETEE EASIGSSVYV
PADRAEDNQL QFAIDLILGE AEDPAFPPNP DAVIAQQDAE NAEVTESP
//
