ID A0A073KSL2_9BACI Unreviewed; 493 AA.
AC A0A073KSL2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:KEK25378.1};
GN ORFNames=BAGA_12185 {ECO:0000313|EMBL:KEK25378.1};
OS Bacillus gaemokensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574375 {ECO:0000313|EMBL:KEK25378.1, ECO:0000313|Proteomes:UP000027778};
RN [1] {ECO:0000313|EMBL:KEK25378.1, ECO:0000313|Proteomes:UP000027778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15801 {ECO:0000313|EMBL:KEK25378.1,
RC ECO:0000313|Proteomes:UP000027778};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus gaemokensis JCM 15801 (MCCC 1A00707).";
RL Submitted (JUN-2014) 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:KEK25378.1}.
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DR EMBL; JOTM01000002; KEK25378.1; -; Genomic_DNA.
DR RefSeq; WP_033673230.1; NZ_LTAQ01000012.1.
DR AlphaFoldDB; A0A073KSL2; -.
DR STRING; 574375.AZF08_07150; -.
DR eggNOG; COG0793; Bacteria.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000027778; 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; 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:SF29; CARBOXY-TERMINAL PROCESSING PROTEASE CTPB; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 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};
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 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..182
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 493 AA; 54155 MW; 795F920ABA940F42 CRC64;
MPFATPPVCF GKGNSALKRR VAIIGMVIAF LIGAGGMFAG MYVFSNNPYM AQTITGDSAG
TKQGDLAKIN EAYALIDSRY VEDVKDDKLV EGAIQGMLSM LKDPYSTYMD KETAKQFEQS
LDPELEGIGA EVNKTEGKLI IVSPIKGSPA EKAGIKPNDQ ILSVDGNSVK DLSREEAVLK
IRGKKGTTVA IEIKRAGVTD PLEFKIKREK IPIFTVFSSV KKEKEKDIGY IQITSFSENT
AKEFKDQLKE LEKKDIKGLV IDVRGNPGGY LNSVEDILGV IMTDKKPMLQ VEQRNGEKKK
FSTSLKERKA YPISVLIDNG SASASEILAG ALKEGEGYDL VGEKTFGKGT VQQAVPFKDG
SNIKLTMFKW LTPDGNWIHK KGIAPTVEVK QPDYYHATPI QIEKTLSYNA NDVQVKHAQE
MLKSLGYVTG REDGYFSKET ESALKAFQNA NEMEATGQLD KKTAEAIQNK IIEKIRSGEN
DLQLQAALKL IAK
//
