ID R0EE75_CAUVI Unreviewed; 463 AA.
AC R0EE75;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=C-terminal processing peptidase {ECO:0000313|EMBL:ENZ80374.1};
DE Flags: Precursor;
GN ORFNames=OR37_03689 {ECO:0000313|EMBL:ENZ80374.1};
OS Caulobacter vibrioides OR37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ80374.1, ECO:0000313|Proteomes:UP000013063};
RN [1] {ECO:0000313|EMBL:ENZ80374.1, ECO:0000313|Proteomes:UP000013063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR37 {ECO:0000313|EMBL:ENZ80374.1,
RC ECO:0000313|Proteomes:UP000013063};
RX PubMed=23792749;
RA Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA Palumbo A.V., Brown S.D.;
RT "Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
RT Tolerant to Heavy Metals.";
RL Genome Announc. 1:0-0(2013).
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:ENZ80374.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APMP01000033; ENZ80374.1; -; Genomic_DNA.
DR RefSeq; WP_004623317.1; NZ_APMP01000033.1.
DR AlphaFoldDB; R0EE75; -.
DR STRING; 1292034.OR37_03689; -.
DR PATRIC; fig|1292034.3.peg.3662; -.
DR eggNOG; COG0793; Bacteria.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000013063; 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:SF30; CARBOXY-TERMINAL PROCESSING PROTEASE CTPA; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|RuleBase:RU004404};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..463
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004340486"
FT DOMAIN 87..169
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 388..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 48931 MW; 0F13D67450371409 CRC64;
MRKYLLIGVS AFVLGAGAMA YVSPIAQANN APKAKTYKML ELFGDVLGTV EDQYVTEVDD
KKLIEAALDG MLTSLDPHSG YLAPDAYEDM QDTTRGEYGG LGIEVTSEDG VVKVISPMDG
TPAARAGIQA GDYITAVNGQ SVLGLTVNEA VKQMRGAPGE AVTLTIARDK TDPFDVKLIR
EVIKPKATIA RMEGDYGYVR LPGFNEKATE ALIASINDLK AKNPHMKGLI FDLRNNPGGL
LDQAVGVADV FLDGGEVVSQ RGRDPRNIQR YNAKPGDLLN GLPMVVLINQ GSASAAEIVA
GALQDRHRAE LVGITSFGKG SVQTVIPLRG GADGALKLTT ARYYTPSGRS IQKTGITPDL
EVAQTRDQAQ DIANRVWFSE ASFKNALNAD EGKTRQGVHN PAEAPPAGFD DKKGDFQLQR
AIAVLKAGGV ANVPKLPKPA AKIAEVTAKA AAAAGKGPPV QEK
//