ID A0A1Y0EFJ0_9RHOB Unreviewed; 806 AA.
AC A0A1Y0EFJ0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative CtpA-like serine protease {ECO:0000313|EMBL:ARU02199.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:ARU02199.1};
GN ORFNames=LOKVESSMR4R_02908 {ECO:0000313|EMBL:ARU02199.1};
OS Yoonia vestfoldensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=245188 {ECO:0000313|EMBL:ARU02199.1, ECO:0000313|Proteomes:UP000195273};
RN [1] {ECO:0000313|EMBL:ARU02199.1, ECO:0000313|Proteomes:UP000195273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMR4r {ECO:0000313|EMBL:ARU02199.1,
RC ECO:0000313|Proteomes:UP000195273};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Loktanella vestfoldensis Strain SMR4r Isolated from a
RT Culture of the Diatom Skeletonema marinoi.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP021431; ARU02199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0EFJ0; -.
DR STRING; 1122181.GCA_000382265_00242; -.
DR KEGG; lvs:LOKVESSMR4R_02908; -.
DR Proteomes; UP000195273; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd12797; M23_peptidase; 1.
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 Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011055; Dup_hybrid_motif.
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; SSF51261; Duplicated hybrid motif; 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:ARU02199.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ARU02199.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..806
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012598205"
FT TRANSMEM 299..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..516
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 726..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 85325 MW; 2826C4F8D4789112 CRC64;
MRWAAILILL ALPAAAQQSA DDAARQLLAA NAQLGAAEGA ADQVAALTQT VQAYEAGLLA
MRQSLREITA AEAEVAADLA ARRDEIAGFL MVLASIGQSP QPVMLANPEG PVGAVRAGMI
IADLTPALRD DVIRLQREFD RLRDLRDRRI AAAEMLREGL DFAQTARAAL GRAISERQDV
PRRFVEDPAQ SAQRLASAQT LAALASELAG LDMPAQTDLA PAADLPLPVA GIIRTGTPDR
PGITIAAAPQ ALVTSPVRAT LLFRGPLLDY GNVVILEPAE DVLFVIAGMA EAFGQPGEII
AAGAPLGLMG GTSAWMTLIL VTIRRLMPVR PRSPFILRSG MGKLRSTRMH GSRWNRMGKP
MNKLMMAATG GAVLGLLVTS QVAGPLLAQE QGQQTSVYEQ LDLFGDIFER IRAGYVEEVD
DRELIEAAIN GMLTSLDPHS SYLSAEDAAA MRVQTSGEFG GLGIEVTQEE GWVKVVSPMD
GTPADVAGIM AGDFITAVDG ESVMGLTLDD AVNLMRGPVG SEIVITVVRE GEVEPFEVSI
IRDTIKLTAV RTRTEGDAVV LRVSTFNEQT FPNLRDGMAE QVAAAGGLDN IDGIVLDLRN
NPGGLLSQAI YVADAFLDAG EITSTRGRNP EDGERFNATS GDLAEGKPIV VLINGGSASA
SEIVAGALQD HRRAIIVGTN SFGKGSVQTV VPLRGEGAMR LTTSRYYTPS GRSIQALGIS
PDIIVEQPRP QPATDEEDDA PATRSEADLR GALNNGLSED QLRQVEQERA RAETAAQLRE
QDYQLAYAID ILKGLNALGP LANGAD
//