ID Q81HB4_BACCR Unreviewed; 530 AA.
AC Q81HB4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=S-layer protein / N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AAP07889.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:AAP07889.1};
GN OrderedLocusNames=BC_0902 {ECO:0000313|EMBL:AAP07889.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP07889.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP07889.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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DR EMBL; AE016877; AAP07889.1; -; Genomic_DNA.
DR RefSeq; NP_830688.1; NC_004722.1.
DR RefSeq; WP_000875317.1; NC_004722.1.
DR AlphaFoldDB; Q81HB4; -.
DR KEGG; bce:BC0902; -.
DR PATRIC; fig|226900.8.peg.847; -.
DR HOGENOM; CLU_029344_0_0_9; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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; PTHR30032:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE CWLM; 1.
DR PANTHER; PTHR30032; N-ACETYLMURAMOYL-L-ALANINE AMIDASE-RELATED; 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; PS51272; SLH; 3.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AAP07889.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..530
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004299260"
FT DOMAIN 25..88
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 89..148
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 149..209
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 530 AA; 58834 MW; 37E448FB109D2598 CRC64;
MKYKAIAAGL LAAHLLAHPI SSLAETKKFP DVSDSAWSKD AIYYLVERNV INGMPDGNFM
PYGNLTRAQA AKIIATAIGA KVDPNAKPSY NDAKNSWAAS FIAAMEKENI IKGREPGVFD
PEGKVTRAEM AAMLVRAYNL KSKVTGPVPT KFADLENHWG KEEVNILVEL KLSLGTENGW
KPNDSITREQ AAQLTAQTDK FSKNSDRPVE TKKMYIDRKF ITYHAPSLSS GISANQHNPQ
TVEIKEERDG WIKIATSNGD KWTPLVEKTE VINEGFTTYA EASSSSKVMG THNAQQVTVI
EENGSWIRIR MGAGFQWVNK NQLNPVKQGN FLEGKAIIID PGHGGVDPGH SGVKMDESAI
VLDTSLRVQK LFEQKTPFTV LLTRNDDTRP GNTPGESLKK RVEFAQENKG DIFVSIHANG
FNEQVEGTET FYYRSATNPN SEESRVLAEK VQKRLVQALQ SNDRGVKTEN FYVVKYNTMP
AILAELGFID AKGEGEKLAT EEWRQRAAEA IYQGILDYYE EMGNNVSSFR
//
