ID E6SBW4_INTC7 Unreviewed; 321 AA.
AC E6SBW4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Lytic transglycosylase catalytic {ECO:0000313|EMBL:ADU48473.1};
GN OrderedLocusNames=Intca_1962 {ECO:0000313|EMBL:ADU48473.1};
OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS 12989 / 7 KIP).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU48473.1, ECO:0000313|Proteomes:UP000008914};
RN [1] {ECO:0000313|EMBL:ADU48473.1, ECO:0000313|Proteomes:UP000008914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC {ECO:0000313|Proteomes:UP000008914};
RX PubMed=21304734; DOI=10.4056/sigs.1263355;
RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL Stand. Genomic Sci. 3:294-303(2010).
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP002343; ADU48473.1; -; Genomic_DNA.
DR RefSeq; WP_013492788.1; NC_014830.1.
DR AlphaFoldDB; E6SBW4; -.
DR STRING; 710696.Intca_1962; -.
DR KEGG; ica:Intca_1962; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_047400_0_0_11; -.
DR Proteomes; UP000008914; Chromosome.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008914}.
FT DOMAIN 26..71
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 100..144
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 73..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 321 AA; 33729 MW; F95B21849AF3F7E9 CRC64;
MLTADVAQLA PPAHIVFAEQ AARPWRAITV RPGDTIWDLA MAHRTTPGAL VSKNRLVGGG
SVIHPGQRLL VPAAPSAGSA SRTGSSRSSA PATATRSSGR FHVVRPGDTL SGIAAANRTS
VTKLLSANRL ADPRMIHPGQ RIALPGRAAP VAPKSSSKPA PTSENTFAGY TYSDATVAAA
KKNRTTLTKA SVPSRSETAS MIRRTAVRHG VDPRLALAIA WQESGWNQRA VSVANAIGTM
QVIPSSGEWA SQLAGRRLDL LDTQDNITAG VVIIRALRVS SGSVKEAIAG YYQGLHSVRT
QGMFADTKQY VAAVLAHAQR M
//
