ID E6VPC5_RHOPX Unreviewed; 372 AA.
AC E6VPC5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:ADU43674.1};
GN OrderedLocusNames=Rpdx1_2066 {ECO:0000313|EMBL:ADU43674.1};
OS Rhodopseudomonas palustris (strain DX-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU43674.1, ECO:0000313|Proteomes:UP000001402};
RN [1] {ECO:0000313|Proteomes:UP000001402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA Woyke T.;
RT "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP002418; ADU43674.1; -; Genomic_DNA.
DR AlphaFoldDB; E6VPC5; -.
DR STRING; 652103.Rpdx1_2066; -.
DR KEGG; rpx:Rpdx1_2066; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_2_0_5; -.
DR Proteomes; UP000001402; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 271..354
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 372 AA; 38822 MW; 75BBB8AE5938FAD7 CRC64;
MRRAQRTDLL LRIAIVWLLV LATFWVAQPY LSALWFSATG PRTVTARGEL APAEKATVEL
FKQVSPSVVH VFAQAQQRVS PFFAQQEAPV QSGSGAIWDA AGHVVTNNHV VQNAGQLGVR
LASGEFVTAR VVGAAPNYDL AVLQLERPQT PLRPIAIGSS EDLQVGQAAY AIGNPYGLEQ
TLTTGIVSAL RRRLPTAAAH EVRGVIQTDA AINPGNSGGP LLDSAGRLIG INTAIISGSG
ASAGIGFAIP VDAVNRVVTA LITNGTVPVP GIGIIAAREN ETAQLGIDGV VVLRTLPDSP
AARAGLEGAT NDGYVRDVIT AADGKPIHGM SDLAAALEEA GIGRDVKLTV ERDGRTRSVT
VKVTDISQQR RG
//
