ID A5HXX6_CLOBH Unreviewed; 352 AA.
AC A5HXX6; A7FZZ9;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Exported protein {ECO:0000313|EMBL:CAL81635.1};
GN OrderedLocusNames=CBO0079 {ECO:0000313|EMBL:CAL81635.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL81635.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL81635.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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DR EMBL; AM412317; CAL81635.1; -; Genomic_DNA.
DR RefSeq; WP_011947942.1; NC_009698.1.
DR RefSeq; YP_001252627.1; NC_009495.1.
DR RefSeq; YP_001386037.1; NC_009698.1.
DR AlphaFoldDB; A5HXX6; -.
DR GeneID; 5184334; -.
DR KEGG; cbh:CLC_0126; -.
DR KEGG; cbo:CBO0079; -.
DR PATRIC; fig|413999.7.peg.79; -.
DR HOGENOM; CLU_036884_0_1_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IBA:GO_Central.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IBA:GO_Central.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR CDD; cd22786; DPBB_YuiC-like; 1.
DR Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR InterPro; IPR010611; 3D_dom.
DR InterPro; IPR007137; DUF348.
DR InterPro; IPR011098; G5_dom.
DR InterPro; IPR026044; MltA.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR30124; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR PANTHER; PTHR30124:SF0; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR Pfam; PF06725; 3D; 1.
DR Pfam; PF03990; DUF348; 2.
DR Pfam; PF07501; G5; 1.
DR SMART; SM01208; G5; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR PROSITE; PS51109; G5; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..230
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
SQ SEQUENCE 352 AA; 38383 MW; 3690374EFD93AF84 CRC64;
MVEKLKKKIK EHFSNGPKAI LIVVVILMIA SIVITNMRKT IIVSIDGKES QKITTFKKTY
AKALTSKNIQ VGPKDKVQPQ LDAEIKDGSK LSIKKAVKVN VEVDGKKLAI QSAENNIGDM
LKKEGIQVKK LDKVAPSKEE EIKKGLKVTV TRVEEKVIKS KKNMDYETVV KEDDSLEKGD
KKVIREGQNG EKEVTTKVVF EDGKEKVRKV VSESIKKQPV SKVVAMGTKV TTVNALSRGG
SVTGTPGGRL LRMRATAYTS SYEDTGKSPG SPDFGVTATG TTARRNSGGY SSIAVDPRVI
PLGTKLFVEG YGYAIAEDTG GAIKGNVIDL YFDSNVEVSN WGSRWVNVYI LD
//
