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Database: UniProt
Entry: R0EE75_CAUVI
LinkDB: R0EE75_CAUVI
Original site: R0EE75_CAUVI 
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}.
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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
//
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