ID A0A3D8GQ94_9BACI Unreviewed; 500 AA.
AC A0A3D8GQ94;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:RDU36451.1};
GN ORFNames=DRW41_13035 {ECO:0000313|EMBL:RDU36451.1};
OS Neobacillus piezotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=2259171 {ECO:0000313|EMBL:RDU36451.1, ECO:0000313|Proteomes:UP000257144};
RN [1] {ECO:0000313|EMBL:RDU36451.1, ECO:0000313|Proteomes:UP000257144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-04 {ECO:0000313|EMBL:RDU36451.1,
RC ECO:0000313|Proteomes:UP000257144};
RA Yu L., Tang X.;
RT "Bacillus sp. YLB-04 draft genome sequence.";
RL Submitted (JUL-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:RDU36451.1}.
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DR EMBL; QNQT01000005; RDU36451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8GQ94; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000257144; 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: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 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 Reference proteome {ECO:0000313|Proteomes:UP000257144};
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 35..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..191
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 54966 MW; 268C9A69D186890E CRC64;
MEVVKAVDEQ NQVQEQEQNS GLREKSPVIR MKRPYFIMLL VFLVIFASGI TAFALSFGKE
SQPMVIGGSS ERDEFAKLYN AYDTLKKGYY KDIDEDKVIN GAINGMIQSL DDPYSTYMDE
KDAKEFQHSV SSSFEGIGAE IQEKDGHIMI VSPLKGSPAE KAGLKPKDIV IMVDGKSIQG
MTSTQAVMLI RGEKGTKVEL TIQRPGVEGT IKVPIIRDEI PIETVHGEMV GDGIAKVQIT
TFSTNTSKEL VETLNNLQEK GMKGLILDLR QNPGGLLEQA VSISSMFVPK GKLLFKVEER
NGNIEEYKSK NEGNPEFPLV VLIDNGSASA SEILAGAVKE SAGVPLVGEK SFGKGTVQTV
QDFPDGSNVK FTTAKWLTPN GNWIHKKGIE PDYKVAVPDY YNLPYLDPKL ELKKGSSSND
VKTAQQMLSV LGFDPGRKDG FFDEKTENAV KAFQQANKLQ TNGAITGSTT EKIIGQLQEK
IIKDDPQLKK AIEVIKKEMK
//