ID Q1D731_MYXXD Unreviewed; 801 AA.
AC Q1D731;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Transglycosylase SLT domain protein {ECO:0000313|EMBL:ABF87753.1};
GN OrderedLocusNames=MXAN_3344 {ECO:0000313|EMBL:ABF87753.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF87753.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF87753.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP000113; ABF87753.1; -; Genomic_DNA.
DR RefSeq; WP_011553378.1; NC_008095.1.
DR AlphaFoldDB; Q1D731; -.
DR STRING; 246197.MXAN_3344; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; ABF87753; ABF87753; MXAN_3344.
DR GeneID; 41360695; -.
DR KEGG; mxa:MXAN_3344; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_013746_1_0_7; -.
DR OrthoDB; 9781970at2; -.
DR Proteomes; UP000002402; 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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR011990; TPR-like_helical_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 Pfam; PF13432; TPR_16; 2.
DR SUPFAM; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..801
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004188281"
FT DOMAIN 644..755
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT REGION 21..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 87958 MW; 063F342810EC2D10 CRC64;
MKPFLSKLAV AASALLMTAQ APAPKAVSST PAEPEASEAP AQHPSNAPSE AQLSPPPDSE
KAPLPVGYVE VLNPAFPNAA PPTPVVHRGR RYALEDLAPY FGEGKKKEAR DAFDRGQYTR
ARELLKDEGD SPPVRYLRAL AAVRAGDDAS AAKEFAALVP DYPALKDRCL THGGVALESL
RRFDEAAVLL EQVPPESKLY VDARLALSRV LRKKKDAAGA MAALEPLTSR AAPSWGRNVG
AEALMAIADI AAEKKDKAAE RAALWRLWAA HPLSALSKQA EKRLKGQTPP VDARVGRGEA
LVELHRNKAG LEQLEPLLPK LALPDPLACR AHFAFGKGMR KERQHTRAIQ VLTPVAEKCQ
DRDLLARVLY VLGSSRSIVD QARGTETYER LAREFPDHSF ADDGLFYAAD LYLKTGRPKE
AMARLDTLAR LYPQGDFLGE ALFKAFWIAR TTGVEDSGLS FLDRIEAQFA KADESYDVER
ARYWRARTMQ EKGNIQGAAE LFEKLSVDHP ATYYGLMARS QLAKVDPPRL EKVSAEIFAV
PEAASPWPLF AGPMGEDPHF RAGVELYRLG FKEAVSSEML AVNRTNLPAE SVRLLVLVLH
EAGDERSAHA VARLALRKDL SGRITPETRV VWEVAYPNAF RDSIEKHTAD AGVEPDLLQA
LMREESALDP KALSWAGAMG LTQLMPSTAK GVARELKLKR FSVDQLLQPD LNIRMGAHYL
GGLLKRFNGH TPYAVGSYNA GPGAVNRWRS DRPDLALDAW VEEIPISETR GYIKRVLRSF
NTYQLLYGRA PKLPVLKSAA K
//
