ID A0A126RCT7_9SPHN Unreviewed; 450 AA.
AC A0A126RCT7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:AMK19385.1};
GN ORFNames=K663_15035 {ECO:0000313|EMBL:AMK19385.1};
OS Sphingobium sp. MI1205.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=407020 {ECO:0000313|EMBL:AMK19385.1, ECO:0000313|Proteomes:UP000060707};
RN [1] {ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|Proteomes:UP000060707};
RA Tabata M.;
RT "Genome sequence of gamma-HCH degrading bacterium Sphingobium sp. MI1205.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMK19385.1, ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|EMBL:AMK19385.1,
RC ECO:0000313|Proteomes:UP000060707};
RX PubMed=27056230;
RA Tabata M., Ohhata S., Nikawadori Y., Sato T., Kishida K., Ohtsubo Y.,
RA Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane-Degrading
RT Bacterium, Sphingobium sp. Strain MI1205.";
RL Genome Announc. 4:0-0(2016).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP005188; AMK19385.1; -; Genomic_DNA.
DR RefSeq; WP_062119332.1; NZ_CP005188.1.
DR AlphaFoldDB; A0A126RCT7; -.
DR STRING; 407020.K663_15035; -.
DR KEGG; spmi:K663_15035; -.
DR PATRIC; fig|407020.3.peg.3144; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000060707; Chromosome 1.
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};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:AMK19385.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..450
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007273316"
FT DOMAIN 83..155
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 345..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 48734 MW; D777C1E52191AC11 CRC64;
MTSNFFRGAI ALGALALIPA TTAALADGEA SSYKALDEFM DVFQKVRSDY VEKVDDEKLI
KGAIDGMLAS LDPHSSFLDA RDFQNLRTQT EGSYGGLGLS VTQEDGAVKV IAPTQDTPAW
RAGIKAGDYI THLDGQLIYG GTLDEAVDKM RGAPGTAIKL TIVRPGRDKP IELTLTREII
QLKPVKWEVK NGVGIINIVS FSANTGADVR QAIRSIDKSL GRKPTGYILD LRSNPGGLLD
EAVSVSDSFL ERGEIVSQRG RNKSDVERYY AKPGDDAKGL PVIVLVDAGS ASASEIVAGA
LQDQRRALVM GERSFGKGSV QTMLPLTNTT ALKLTTARYY TPSGKSVQEG GIEPDVRVPQ
LSDPDYKNRP KFRESDLRRH LINEIKTDNA ALEEDTKEDP RFSMSAEELK KKGIEDFQLD
YALKTIGRLA AKPGAVVAQA QPIAKKAPLR
//
