ID B9IXG6_BACCQ Unreviewed; 432 AA.
AC B9IXG6;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Stage IV sporulation protein B {ECO:0000313|EMBL:ACM14387.1};
GN Name=spoIVB {ECO:0000313|EMBL:ACM14387.1};
GN OrderedLocusNames=BCQ_3959 {ECO:0000313|EMBL:ACM14387.1};
OS Bacillus cereus (strain Q1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM14387.1, ECO:0000313|Proteomes:UP000000441};
RN [1] {ECO:0000313|EMBL:ACM14387.1, ECO:0000313|Proteomes:UP000000441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1 {ECO:0000313|EMBL:ACM14387.1,
RC ECO:0000313|Proteomes:UP000000441};
RX PubMed=19060151; DOI=10.1128/JB.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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DR EMBL; CP000227; ACM14387.1; -; Genomic_DNA.
DR AlphaFoldDB; B9IXG6; -.
DR MEROPS; S55.001; -.
DR KEGG; bcq:BCQ_3959; -.
DR HOGENOM; CLU_035713_0_0_9; -.
DR Proteomes; UP000000441; Chromosome.
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; PS51257; PROKAR_LIPOPROTEIN; 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 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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..432
FT /note="Peptidase S55"
FT /evidence="ECO:0000259|PROSITE:PS51494"
FT REGION 398..400
FT /note="PDZ binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT ACT_SITE 368
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT ACT_SITE 383
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
SQ SEQUENCE 432 AA; 47032 MW; 9CCEC7D9ECCFEF1F CRC64;
MNKLKLERFR KIIGIFLLVS LVFIGCFKPL RTFISSPKQL VVFEGQQSEI ASLPVFKASS
TDRHVFTVSS NEQKQGLMVN SHQNGEADMV FQLAGFPVKK VNVRVLKDFK VIPGGQSIGV
KLNTKGILVV GHHLIQTEKG KVSPGETAGV QIGDMITEIN GKTIERMSDV APFIHNSGET
GEPLNLVLLR DGKHIRTKLT PQKDSGESSY RIGLYIRDSA AGIGTMTFVH PDSMKYGALG
HVISDNDTKK PIQVEDGQIM RSTVTSIERG SHGNPGEKLA RFSPDREVIG NITINSPFGI
FGKLNTNMTN GVMDKAMPIA LSHQVKEGPA KILTVIDQDK VEAFDIEVVS TVPQKFPATK
GMVIKVTDKR LLAKTGGIVQ GMSGSPIVQN GKVIGAVTHV FVNDPTSGYG VHIEWMLHEA
GINIYDQERK AS
//
