ID R7Z7X1_LYSSH Unreviewed; 497 AA.
AC R7Z7X1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Periplasmic protease {ECO:0000313|EMBL:EON70280.1};
GN ORFNames=H131_22179 {ECO:0000313|EMBL:EON70280.1};
OS Lysinibacillus sphaericus OT4b.31.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON70280.1, ECO:0000313|Proteomes:UP000013911};
RN [1] {ECO:0000313|EMBL:EON70280.1, ECO:0000313|Proteomes:UP000013911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT4b.31 {ECO:0000313|EMBL:EON70280.1,
RC ECO:0000313|Proteomes:UP000013911};
RA Pena-Montenegro T.D., Dussan J.;
RT "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT sphaericus strain OT4b.31.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:EON70280.1}.
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DR EMBL; AQPX01000040; EON70280.1; -; Genomic_DNA.
DR RefSeq; WP_010861332.1; NZ_KB933415.1.
DR AlphaFoldDB; R7Z7X1; -.
DR PATRIC; fig|1285586.5.peg.4624; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_3_0_9; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000013911; Unassembled WGS sequence.
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; 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; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
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 Pfam; PF01471; PG_binding_1; 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 SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:EON70280.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..188
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54389 MW; 9C24458159697FF2 CRC64;
MDEQKKDDLE QQEQTPQGEV KPAGQFIQMK PFKFIMLMFF TILITAGLTI FALTFGEKKV
VEVKVPIERA EFTKLYEAFD MLKSKYYKDI EDEKVVDGAI NGMFDALDDP YSDFMVKDEA
EKFNTGLSSS FQGIGAEIQE RNGFITVVSP IKNSPAEKAG LLPKDIILTV DGKSIQGFSS
SEAVALIRGE KGTPVKLTVK RGENAEPIQM TIVRDDIPVE TVYGEMLDGD IAHIQITSFS
EQTADELEKI LAEYEGKGMK GIVLDLRQNP GGYLDAALEI SNLFVAEGKP IVQVQEKDEE
PAIKNAIGGK KYNLPVTVLV DNGSASASEI LAAALSESVG AKIVGETSFG KGTVQNVTPL
KDGSNLKFTT GKWLTPNGNW INEKGIEPDV KVPYPPYASL PFLDASYEMK KGLQSESVKA
AEEMLEVLGY DPGKVDGVFD QYTERAVEKL QAASKLEETG VLTGETTYAL MDALRIKMKS
DDPQLLKAKE LLTGGKE
//
