ID A0A176JBI0_9BACI Unreviewed; 441 AA.
AC A0A176JBI0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=SpoIVB peptidase {ECO:0000313|EMBL:KZZ86243.1};
GN ORFNames=AS29_001320 {ECO:0000313|EMBL:KZZ86243.1};
OS Bacillus sp. SJS.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ86243.1, ECO:0000313|Proteomes:UP000028527};
RN [1] {ECO:0000313|EMBL:KZZ86243.1, ECO:0000313|Proteomes:UP000028527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJS {ECO:0000313|EMBL:KZZ86243.1,
RC ECO:0000313|Proteomes:UP000028527};
RA Newman J.D., Stropko S.J., Pipes S.E.;
RT "Bacillus sp. SJS genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZZ86243.1}.
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DR EMBL; JAQV02000003; KZZ86243.1; -; Genomic_DNA.
DR RefSeq; WP_051860475.1; NZ_JAQV02000003.1.
DR AlphaFoldDB; A0A176JBI0; -.
DR STRING; 1423321.AS29_001320; -.
DR eggNOG; COG0750; Bacteria.
DR OrthoDB; 9765242at2; -.
DR Proteomes; UP000028527; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR008763; Peptidase_S55.
DR InterPro; IPR014219; SpoIVB.
DR NCBIfam; TIGR02860; spore_IV_B; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF05580; Peptidase_S55; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51494; SPOIVB; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00827};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00827};
KW Reference proteome {ECO:0000313|Proteomes:UP000028527};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU00827}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 114..200
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 201..440
FT /note="Peptidase S55"
FT /evidence="ECO:0000259|PROSITE:PS51494"
FT REGION 406..408
FT /note="PDZ binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT ACT_SITE 249
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT ACT_SITE 376
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT ACT_SITE 391
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
SQ SEQUENCE 441 AA; 47441 MW; E71A269F0AA0758A CRC64;
MVWVRSEESE SVSFEKIRKI IGVILLVSLI SIGFLKPVKE YIQLPKTVTI FESQTASLAS
AMPVQAAAAG SHTEAFSVHQ TNTEVKLKGE KAGESSVVFE WGGMPVKKTE VRVLPNLKVI
PGGQSIGVKL NTLGVLVVGH HQVNTAEGKQ SPGEIAGVQV GDIITEINGT KIEEMNDVTP
FIESSGKTGK PLNLVIYRDN QSHKAKLYPL KDEGDQAYRI GLYIRDSAAG IGTMTFIEPQ
SQKYGALGHV ISDMDTKKPI VVHDGEVMRS TVTSIEKGNN GNPGEKRARF SSDRVIVGDI
SRNSPFGIFG RLNQGMSNGI ADKPLPVALS HEVKEGPAKI LTVVEDDKVE AFDVKIVSTI
PQKFPATKGL VLKVTDPKLL EKTGGIVQGM SGSPIIQNGK VIGAVTHVFV NDPTSGYGVH
IEWMLNEAGI NLYKEKVQAA S
//
