ID A0A098M933_9BACL Unreviewed; 545 AA.
AC A0A098M933;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KGE18566.1};
GN ORFNames=PWYN_03680 {ECO:0000313|EMBL:KGE18566.1};
OS Paenibacillus wynnii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=268407 {ECO:0000313|EMBL:KGE18566.1, ECO:0000313|Proteomes:UP000029734};
RN [1] {ECO:0000313|EMBL:KGE18566.1, ECO:0000313|Proteomes:UP000029734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE18566.1,
RC ECO:0000313|Proteomes:UP000029734};
RA den Bakker H.C.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGE18566.1, ECO:0000313|Proteomes:UP000029734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE18566.1,
RC ECO:0000313|Proteomes:UP000029734};
RA Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:KGE18566.1}.
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DR EMBL; JQCR01000002; KGE18566.1; -; Genomic_DNA.
DR RefSeq; WP_036648605.1; NZ_JQCR01000002.1.
DR AlphaFoldDB; A0A098M933; -.
DR STRING; 268407.PWYN_03680; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000029734; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KGE18566.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029734};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 442..524
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 57662 MW; 0FA548C25CF0D75C CRC64;
MNDNKDRFTR ENEPAPDREW NGSTTNENSG GGQSSESGSS YYYSYGPFKS INQDNSDGIE
HYNRREPERV EVTPPPTVKP VPYSTSIRTT GFDGSGGGRN GNGGNGSDGG NGWQYNRKPK
SSFKSILISF LAGMVVLSGS MFAADRGNWF TGDSEEPAVT AGATAPDEGA NVSPATATTS
LNSGANDVSS VVDGVGPAVV KIETLVNSSS RGGSQSNPNM SDPFSQFFFG DQFGGSGSSE
QTEPEPKSYS STQLIPNSVG TGFIYDKAGY ILTNQHVING ADVIQVTIEG NKKPYEAKLL
GSSKDLDLAV LKIEGDNNFP AVAMGDSDTL KVGSEVVAIG NPQGFDHTVT AGVLSAKGRS
IDINEEDGSG TRNYKDLLQT DASINPGNSG GPLLNMKGQV IGMNVAVSTD SQGIGFAIAV
NTIKEVVQKL EDNQAIPKEP VPFIGATLMT ITDEVAKQMG TDIKEGSVVA EIIYKSPAYV
ADLRPYDIIS GVNGKNYATS QDLIDFIRTL KVGDKATLNV VRDDKKLELP ITIGNKNDFV
TSKTE
//
