ID Q65I05_BACLD Unreviewed; 321 AA.
AC Q65I05; Q62TF3;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Spore cortex-lytic enzyme {ECO:0000256|ARBA:ARBA00018364};
GN Name=sleB {ECO:0000313|EMBL:AAU23956.1};
GN OrderedLocusNames=BL02222 {ECO:0000313|EMBL:AAU23956.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU23956.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU23956.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- SIMILARITY: Belongs to the SleB family.
CC {ECO:0000256|ARBA:ARBA00007010}.
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DR EMBL; CP000002; AAU23956.1; -; Genomic_DNA.
DR RefSeq; WP_011198075.1; NC_006322.1.
DR AlphaFoldDB; Q65I05; -.
DR STRING; 279010.BL02222; -.
DR KEGG; bli:BL02222; -.
DR PATRIC; fig|279010.13.peg.2462; -.
DR eggNOG; COG3409; Bacteria.
DR eggNOG; COG3773; Bacteria.
DR HOGENOM; CLU_053345_0_0_9; -.
DR Proteomes; UP000000606; 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:UP000000606};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..321
FT /note="Spore cortex-lytic enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038542501"
FT DOMAIN 42..99
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 222..320
FT /note="Cell wall hydrolase SleB"
FT /evidence="ECO:0000259|Pfam:PF07486"
FT REGION 125..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 321 AA; 35580 MW; FAF8C50F4C24094B CRC64;
MKSKGSFCLN VILCTIMATS LSLPFSQKSA AFSEQVIQRG ATGDDVIELQ ARLQYNGYYN
GRIDGVYGWA TYWAVRNFQN QFGLRDTDGL VGPKTKRLLI NHTKYYSDYV HRQLRKGNQF
THYGGLPLKY QTKPSKEVQQ QARKKAEARQ RQGAQQQGTA QKQPQQKQQA APAQPKKQAQ
PKAAPKQAAP KKQDAVAANM PGGFSNNDIN LLAQAVYGEA RGEPYDGQVA VAAVILNRLD
SPTFPNTVAG VIFEPLAFTA VADGQIYMTP DETAKKAVLD AINGWDPSEN ATYYFNPDTA
TSSWIWGRPQ IKRIGKHIFC E
//