ID A7GLR1_BACCN Unreviewed; 527 AA.
AC A7GLR1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Cell wall hydrolase/autolysin {ECO:0000313|EMBL:ABS21069.1};
DE Flags: Precursor;
GN OrderedLocusNames=Bcer98_0724 {ECO:0000313|EMBL:ABS21069.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21069.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS21069.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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DR EMBL; CP000764; ABS21069.1; -; Genomic_DNA.
DR RefSeq; WP_011983825.1; NC_009674.1.
DR AlphaFoldDB; A7GLR1; -.
DR STRING; 315749.Bcer98_0724; -.
DR GeneID; 56416316; -.
DR KEGG; bcy:Bcer98_0724; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_029344_0_0_9; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000002300; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABS21069.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..527
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002709449"
FT DOMAIN 23..82
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 83..146
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 147..207
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 527 AA; 58668 MW; D037E607E42600AF CRC64;
MNYRKVVAGI LTAAVLSCPT SSLAAGKSFP DVPTWAQDSV NYLVAKNVLD GKPDGTFAPI
EEIDRGSAAK LLASVLGLDV NKEAKPSFTD AQNHWAAPYI AAVEKAGIIV GEGNGKFNPT
GKINRASMAT MLVKAYALEG KVIGEIPNQF DDIKDHWGRK NVNILAALEI SKGKGNVWDP
EGQVTRAEAV QFIAKTDMRK EDTSKRMYMD RPFITYHQPS LSSGITSNQH KPQIIEVKEQ
RKDGWMKIVT STGDKWTPLH EKTEYIGESF TTYQEASHKS TILGKYGPQT VTIMEESGDW
IRIRTNAGFQ WLDKKQLNPP KQANFLEGKA IIIDPGHGDP DPGKDSLYME ESKIVLDTSK
RVKALFEKKT PFTVLLTREG DARPGSSAAD SLKKRVEFAQ RNKADIFVSI HGNAYNGQAN
GTETFYYNSK TKRTNPHVDE SYMLAQKIQK RLVAALGTRD RGVQHKDLYV TRENTMPAVL
TELAFVDNKI EGEKLAQPEW RQRAAEAIYA GILDYYEWKG NDVSAYR
//
