ID A0A0V8S162_9CELL Unreviewed; 551 AA.
AC A0A0V8S162;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidase S1 {ECO:0000313|EMBL:KSW14037.1};
GN ORFNames=ATM99_02985 {ECO:0000313|EMBL:KSW14037.1};
OS Cellulomonas sp. B6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW14037.1, ECO:0000313|Proteomes:UP000054319};
RN [1] {ECO:0000313|EMBL:KSW14037.1, ECO:0000313|Proteomes:UP000054319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:KSW14037.1,
RC ECO:0000313|Proteomes:UP000054319};
RA Piccinni F.E., Campos E.;
RT "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT Isolated from Decaying Forest Soil.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KSW14037.1}.
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DR EMBL; LNTD01000271; KSW14037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V8S162; -.
DR STRING; 1295626.ATM99_02985; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000054319; Unassembled WGS sequence.
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; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
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 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054319};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 127..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 379..477
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 54759 MW; 70C547A993F8DC51 CRC64;
MGVDKEAAMT TTPEPQHGHH PQDHPTQPLP APDATRPLPP QQAAPASGPQ PGAPARLTPA
QQWARYEAAQ RAAQQPTPVG TGAHAPGAAF GVGGPGAPGA VPPGAVPPGT DPWAAPGEPA
PRRRSRAWAW VASAAVVGVL VGGGAVAGVG GLTGALSDPA SSQRSASLAD VGRSTAENVP
VSGSSKDSPD WQAVAAAVQA SVVAIDVTTQ SGEAQGSGVI IDDAGHVLTN NHVVAGAQGN
VQVTLTDGRM FEAQVVGTDA STDLAVVKLV DAPDDLKAAA LGDSDAVAVG DPVMAVGNPL
GLANTVTTGI VSAVDRPVST QENGGEAAVT NAIQIDAAIN PGNSGGPLFD ATGRVIGITS
SIATLSQQSG SIGLGFAIPV NVTKNIAGQL IQDGQAEHAY LGVTLADGTA TADGVTRRGA
VVQTVSDGSP AAAGGLQNGD VIVAIGKDPV GGAESLTAFV RSMASGDDAT LTVVRDSKAI
EVDVKLATRP DTTAQGQQGG QGQQGGQGQQ GGQDQQGQQG GQQGQLPGGM TPEQLWQWFQ
QRQQQEQQGQ G
//
