ID A0A095ZFE9_9BACT Unreviewed; 455 AA.
AC A0A095ZFE9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Murein transglycosylase {ECO:0000313|EMBL:KGF33106.1};
GN ORFNames=HMPREF2137_11835 {ECO:0000313|EMBL:KGF33106.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF33106.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF33106.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF33106.1,
RC ECO:0000313|Proteomes:UP000029556};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF33106.1}.
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DR EMBL; JRNN01000095; KGF33106.1; -; Genomic_DNA.
DR RefSeq; WP_036874735.1; NZ_JRNN01000095.1.
DR AlphaFoldDB; A0A095ZFE9; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000029556; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
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; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..455
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001914296"
FT DOMAIN 411..454
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 372..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..411
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..455
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 51883 MW; 9001C3849FEC0590 CRC64;
MKKIYLFIVT LLVVFSSSLQ AQVVDDDTEI TVTNEKGENE TFDLPEAMTS EIDSLLHLYN
TKTYLKRDAD CNLPNVNKTY EPDVYKDRLR RLPTIMEMPY NNVVQKFIDR YSNELRNAVG
IMLGASNFYM PIFEQALETY NLPLELKYLP VIESGLNPKA VSRVGATGLW QFMLATAKNY
GLEINSLLDE RCDPIKSSYA AANYLSDLYR IFGDWNLVIA AYNCGPDKLT QAIHRAGGSK
DYWKIYPYLP RETRGYVPAF IAANYIMNYY CEHNICPMTT DLPAKTDTIL VNRDVHFKQI
AQVLNMDEEL VRSLNPQYRK DIVIGYTKPS TLRLPVDKIN SFIDQEDSVY AYNADVLLTK
RSEVEVAQGA PNYSIGRTST SSSRKSYSRS KSKRSSRKSS RSSRRRRSSN KSVTVRGGDT
LSEIAARNNT TVKKLKRLNG LKGNNIRKGK KIRVR
//
