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Database: UniProt
Entry: B7GHM7_ANOFW
LinkDB: B7GHM7_ANOFW
Original site: B7GHM7_ANOFW 
ID   B7GHM7_ANOFW            Unreviewed;       305 AA.
AC   B7GHM7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Spore cortex-lytic enzyme {ECO:0000256|ARBA:ARBA00018364};
GN   Name=sleB {ECO:0000313|EMBL:ACJ33449.1};
GN   OrderedLocusNames=Aflv_1073 {ECO:0000313|EMBL:ACJ33449.1};
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ33449.1, ECO:0000313|Proteomes:UP000000742};
RN   [1] {ECO:0000313|EMBL:ACJ33449.1, ECO:0000313|Proteomes:UP000000742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
CC   -!- SIMILARITY: Belongs to the SleB family.
CC       {ECO:0000256|ARBA:ARBA00007010}.
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DR   EMBL; CP000922; ACJ33449.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7GHM7; -.
DR   STRING; 491915.Aflv_1073; -.
DR   KEGG; afl:Aflv_1073; -.
DR   eggNOG; COG3409; Bacteria.
DR   eggNOG; COG3773; Bacteria.
DR   HOGENOM; CLU_053345_0_0_9; -.
DR   Proteomes; UP000000742; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009847; P:spore germination; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 6.20.240.60; -; 1.
DR   Gene3D; 1.10.10.2520; Cell wall hydrolase SleB, domain 1; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR011105; Cell_wall_hydrolase_SleB.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR042047; SleB_dom1.
DR   InterPro; IPR014224; Spore_cortex_SleB.
DR   NCBIfam; TIGR02869; spore_SleB; 1.
DR   Pfam; PF07486; Hydrolase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Germination {ECO:0000256|ARBA:ARBA00022544};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000742};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT   DOMAIN          58..113
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          206..304
FT                   /note="Cell wall hydrolase SleB"
FT                   /evidence="ECO:0000259|Pfam:PF07486"
SQ   SEQUENCE   305 AA;  34204 MW;  1258EA42189D6382 CRC64;
     MYKNVIVTKN SVKRYCLHIK GGVTMRKWFI CLFFIFSFSY TSQVHAFSKQ VIQRGAVGDD
     VIELQARLQY LGFYRGKIDG VFSWRTYWAL RNFQYKFKLP VDGLAGEATK QKLVRASKYY
     KSFVHSNLRK GNTFTHYGGV PLSKQVKARQ TKAKNQVTAT KTTNTRDNSK QMAVKQVKAA
     AVNVPNGFSQ NDIQLMANAV HGEARGEPYI GQVAVAAVIL NRINSPSFPN TVAGVIFEPG
     AFTAVADGQI WLTPNETSRK AVLDALNGWD PSSGALYYFN PNTATNGWIW GRPQIKRIGK
     HIFCK
//
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