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Database: UniProt
Entry: Q97JP1_CLOAB
LinkDB: Q97JP1_CLOAB
Original site: Q97JP1_CLOAB 
ID   Q97JP1_CLOAB            Unreviewed;       253 AA.
AC   Q97JP1;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Predicted lytic murein transglycosylase (N-term. LysM motif repeat domain) {ECO:0000313|EMBL:AAK79204.1};
GN   OrderedLocusNames=CA_C1232 {ECO:0000313|EMBL:AAK79204.1};
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79204.1, ECO:0000313|Proteomes:UP000000814};
RN   [1] {ECO:0000313|EMBL:AAK79204.1, ECO:0000313|Proteomes:UP000000814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC   {ECO:0000313|Proteomes:UP000000814};
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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DR   EMBL; AE001437; AAK79204.1; -; Genomic_DNA.
DR   PIR; A97052; A97052.
DR   RefSeq; NP_347864.1; NC_003030.1.
DR   RefSeq; WP_010964545.1; NC_003030.1.
DR   AlphaFoldDB; Q97JP1; -.
DR   STRING; 272562.CA_C1232; -.
DR   GeneID; 44997739; -.
DR   KEGG; cac:CA_C1232; -.
DR   PATRIC; fig|272562.8.peg.1432; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG3773; Bacteria.
DR   HOGENOM; CLU_053345_1_0_9; -.
DR   OrthoDB; 9785345at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 6.20.240.60; -; 1.
DR   Gene3D; 1.10.10.2520; Cell wall hydrolase SleB, domain 1; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 2.
DR   InterPro; IPR011105; Cell_wall_hydrolase_SleB.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR042047; SleB_dom1.
DR   PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR   Pfam; PF07486; Hydrolase_2; 1.
DR   Pfam; PF01476; LysM; 2.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF54106; LysM domain; 2.
DR   PROSITE; PS51782; LYSM; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000814};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..253
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004321972"
FT   DOMAIN          28..71
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          74..117
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   253 AA;  26927 MW;  5B1A03BD48BB09C3 CRC64;
     MIKSKFKFLV FAAALAFVGM GKNAVHAATY SVKSGDTLYS ISRNYGTNYN YLMSANKLQT
     SAIYAGQSLK VPDVKYTIKS GDTLYSIAKR FGVLLSDLQL ANNISNNIIK VGQVIVIPVN
     TSTAATPSYV ISCTSSEVDL LARLINAEAG GESYNAMVSV GAVIVNRVQS SAFPNTVTGV
     IYQVSNGYYQ FTPVLNGMIN KGATASSLSA AKAALYGSDP TKGALYFYDN TVSNTWLTSK
     PVSLVSGKLI FAY
//
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