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Database: UniProt
Entry: A0A1B1Z5M7_9BACI
LinkDB: A0A1B1Z5M7_9BACI
Original site: A0A1B1Z5M7_9BACI 
ID   A0A1B1Z5M7_9BACI        Unreviewed;       290 AA.
AC   A0A1B1Z5M7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Spore cortex-lytic enzyme {ECO:0000256|ARBA:ARBA00018364};
GN   ORFNames=ABE41_011950 {ECO:0000313|EMBL:ANX12724.1};
OS   Fictibacillus arsenicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX12724.1, ECO:0000313|Proteomes:UP000077412};
RN   [1] {ECO:0000313|EMBL:ANX12724.1, ECO:0000313|Proteomes:UP000077412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-54 {ECO:0000313|EMBL:ANX12724.1,
RC   ECO:0000313|Proteomes:UP000077412};
RA   Zheng Z.;
RT   "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT   toxicity to nematodes and a potential arsenic-resistance activity.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SleB family.
CC       {ECO:0000256|ARBA:ARBA00007010}.
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DR   EMBL; CP016761; ANX12724.1; -; Genomic_DNA.
DR   RefSeq; WP_066290534.1; NZ_CP016761.1.
DR   AlphaFoldDB; A0A1B1Z5M7; -.
DR   STRING; 255247.ABE41_011950; -.
DR   KEGG; far:ABE41_011950; -.
DR   OrthoDB; 9785345at2; -.
DR   Proteomes; UP000077412; 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:UP000077412};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..290
FT                   /note="Spore cortex-lytic enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008533261"
FT   DOMAIN          43..98
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          191..289
FT                   /note="Cell wall hydrolase SleB"
FT                   /evidence="ECO:0000259|Pfam:PF07486"
FT   REGION          133..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   290 AA;  31145 MW;  5796B99526072596 CRC64;
     MKRNSAYIKG AFFAIALCFG LFAGFGQNNA HAFSNQVIQK GATGDDVVEL QSRLQYLGFY
     TGNIDGVFGW RTYWALRNFQ YEFGMDIDGL AGAKAKQKLV KASKYDKAWV TKQINSGNKF
     SYYGGVPKSK QTKSGGAKGG AAKKGTAQGG AGGGKATAKP AQVKPAKNIP DGYSQNDISL
     MANAVYGEAR GEPYIGQVAV AAVIINRVED SQFPKTVSGV IFEPGAFTAV ADGQIYLTPN
     KQAKKAVMDA LNGWDPTGEA IYYFNPDTAT SGWIWGRPQI KKIGKHIFCN
//
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