ID A0A3S0R783_9BACI Unreviewed; 480 AA.
AC A0A3S0R783;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=S41 family peptidase {ECO:0000313|EMBL:RUL54241.1};
GN ORFNames=EK386_06955 {ECO:0000313|EMBL:RUL54241.1};
OS Lysinibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=2498145 {ECO:0000313|EMBL:RUL54241.1, ECO:0000313|Proteomes:UP000287910};
RN [1] {ECO:0000313|EMBL:RUL54241.1, ECO:0000313|Proteomes:UP000287910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYSU K30002 {ECO:0000313|EMBL:RUL54241.1,
RC ECO:0000313|Proteomes:UP000287910};
RA Narsing Rao M.P., Zhang H., Dong Z.-Y., Niu X.-K., Zhang K., Fang B.-Z.,
RA Kang Y.-Q., Xiao M., Li W.-J.;
RT "Lysinibacillus antri sp. nov., isolated from a cave soil.";
RL Submitted (DEC-2018) 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:RUL54241.1}.
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DR EMBL; RYYR01000007; RUL54241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0R783; -.
DR Proteomes; UP000287910; 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; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
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; PF13180; PDZ_2; 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; 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};
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 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..168
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 480 AA; 53219 MW; DB04FD28BF8C93D9 CRC64;
MRKSRIFLLL GAICIIAVSI IVWQKWSATE EVAKVSEVPV IDQAYSLITE KSVYGTAQEK
IIEGALRGMT DAIQDPYSTY YNEKEAALHK QSLAGQRVGI GIEITEKNGK FIVVSPVKSS
PAEKAGIRPF DEIVQVDNER LEGKTIGELM QLIQGEAGQK VTLVLYRPST ERHIKVSVER
AEIANKTVSS KVLPVGKDVE IGYISISMFG EKTAEEWVEA TKKLISEDVE GLIVDLRDNP
GGYLHSVAAV VSSIEKKNQV FAYMQNGAGA MEPLKTVAIE EEKFYLDKMS KLPIVVLQNE
GSASASEVMA GAVQSWERAL VVGGKSFGKG TVQETWDLEN GGEIKLSTNK WLTPNREWIH
GKGIKADIEV EQHPLFSMEV IPITGEFAEG DFSEEVAYSQ KVLSALGYTV NRTDGFYDED
TGDAVALYRE KNDLKEGRYM DNEFFTNVRE QIIKYKEDTD NDAQLNMGLS VMLHRLDGDI
//
