ID D9T561_MICAI Unreviewed; 289 AA.
AC D9T561;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Lytic transglycosylase catalytic {ECO:0000313|EMBL:ADL47871.1};
GN OrderedLocusNames=Micau_4358 {ECO:0000313|EMBL:ADL47871.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL47871.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL47871.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) 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; CP002162; ADL47871.1; -; Genomic_DNA.
DR RefSeq; WP_013287487.1; NC_014391.1.
DR AlphaFoldDB; D9T561; -.
DR STRING; 644283.Micau_4358; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR KEGG; mau:Micau_4358; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_1036777_0_0_11; -.
DR OrthoDB; 5244690at2; -.
DR Proteomes; UP000001908; Chromosome.
DR CDD; cd00254; LT-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
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; PF01464; SLT; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..289
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003128751"
FT DOMAIN 149..262
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT REGION 26..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 30998 MW; 2E01AC96228819C0 CRC64;
MRRGLGRWAV TVVALLAAAT LTACGEEERP VREVAADLPT AAPAEQPQEA PADAPSEEPP
AVAAMGGRPS PSASAKPKPR AKPSRTTTAP LARPKPPTET QVPPAPPKPV DDGCKPSYRG
TKASQSQVKA ALADAAARTY WPTSAPDIRI PSALLKATAW QESGWQSNII ACDGGVGLMQ
VMPATAEWMN QRFGQSYDID AYRDNAYLGG TYLAWLTKYI GDMYFESDYR LDASLCTAEL
NSCLLNAVIA AYNYGHGAVA REDQPLTIPN PQYVRNVRAL MTECECLSF
//
