ID B1Y639_LEPCP Unreviewed; 690 AA.
AC B1Y639;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Lytic transglycosylase catalytic {ECO:0000313|EMBL:ACB32386.1};
DE Flags: Precursor;
GN OrderedLocusNames=Lcho_0111 {ECO:0000313|EMBL:ACB32386.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB32386.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB32386.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP001013; ACB32386.1; -; Genomic_DNA.
DR RefSeq; WP_012345148.1; NC_010524.1.
DR AlphaFoldDB; B1Y639; -.
DR STRING; 395495.Lcho_0111; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR KEGG; lch:Lcho_0111; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_019016_0_0_4; -.
DR OrthoDB; 92254at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR CDD; cd13401; Slt70-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
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; PF01464; SLT; 1.
DR SUPFAM; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001693};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..690
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002770551"
FT DOMAIN 520..623
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 690 AA; 76003 MW; 109B6DA619078C56 CRC64;
MKYLVSLFLG SCALLSPCAA QSPQAVDTAA PALVAEPIAP TGAAALAIRP IDQRLLDARE
ALRSRDRARL ASARDALVAA RHPLAMWADY WEIGLRLGEV GQDDLEAFYA RWPGTYVEDR
LRNDWLLELG IRRDWARFGA ELPRFRMADD RQVNCYAMLL RHQAGDDVRA SARSSWLGQR
EPAAGCALMA GTLFEARRLS SADVWLKARI SAEAGRPKLA REALALISET LADKPLTELW
DQPLRYFNKH ADAGHRQGAE MVVLALVRLA TSDPQTAATL LEDRWQAQLA PDAAAWTWAA
IAKQAAWKRL PEADGWFQRA LTVPQARDVD WSDDTLAWRA RAALRATDAQ RWERVLSAIN
AMTAPAQADP TWVYWKGRAL MATAAAGTDG DARRTGAAVL FERIAGGYNF YGKLAADALG
RTQSLPPRPA ALGADERRAA EQNPGLNRAL MLIGLGLRSE GVREWNFSVI GMNDRALLAA
AQRACEREIW DRCIHTSERT RTEVDMAQRF PTPFRAEVVA AAQEVGLDAA YIYGLIRQES
RFITDVRSSA GAAGLMQLMP GTARWTARKL GVPYTADRIT DRNLNLRLGA GYLKLVLDDF
EGSQALATAA YNAGPSRSRR WREGPPIEVA AWAESIPFNE TRDYVKKVLS NASYYAALLG
GQSVVNLKQR LGPPVTPRAE TALTENRDLP
//
