ID A0A0M9EFD7_9RHOB Unreviewed; 444 AA.
AC A0A0M9EFD7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative CtpA-like serine protease {ECO:0000313|EMBL:KPA20540.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:KPA20540.1};
GN ORFNames=shim_35300 {ECO:0000313|EMBL:KPA20540.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA20540.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA20540.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA20540.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-2015) 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:KPA20540.1}.
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DR EMBL; LAJH01000021; KPA20540.1; -; Genomic_DNA.
DR RefSeq; WP_054003919.1; NZ_LAJH01000021.1.
DR AlphaFoldDB; A0A0M9EFD7; -.
DR STRING; 1389006.shim_35300; -.
DR PATRIC; fig|1389006.3.peg.3638; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000037951; 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; 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; PF13180; PDZ_2; 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:KPA20540.1};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:KPA20540.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037951};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 88..156
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 367..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 47706 MW; F231DBD8CA1ECFFB CRC64;
MKKFVAAAAG GIVAGLLVTT QVAGPLLAQE NDRKANVYQQ LDLFGDIFER IRVQYVEDVD
EGDLIEAAIN GMLTSLDPHS SYLSPDDAED MRVQTRGEFG GLGIEVTQEE GFVKVVSPID
DTPADAAGIE AGDFITHVDG ESVLGLNLDQ AVEMMRGPVG SEIVITVVRE GETEPFDVTI
VRDTIKLTAV RTRTVGDSVV LRVTTFNDQT TPNLETGFAK QVEELGGMDN VNGIVLDLRN
NPGGLLTQAI KVSDSFLEKG EIVSTRGRNP QDGERYNAEP GDLAAGKPIV VLINGGSASA
SEIVAGALQD HRRAIVVGTK SFGKGSVQTV MPLRGEGAMR LTTARYYTPS GRSIQALGVS
PDIVVEQPRR KAASEEEEET SRRFNGEADL RGSLNNDSLT DDEVRQIEED RAKAEDAAKL
REEDYQLAYA LDILKGLSAL GSKE
//
