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Database: UniProt
Entry: Q5LA14_BACFN
LinkDB: Q5LA14_BACFN
Original site: Q5LA14_BACFN 
ID   Q5LA14_BACFN            Unreviewed;       271 AA.
AC   Q5LA14;
DT   21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Peptidoglycan biosynthesis-related protein {ECO:0000313|EMBL:CAH09061.1};
GN   ORFNames=BF9343_3280 {ECO:0000313|EMBL:CAH09061.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH09061.1, ECO:0000313|Proteomes:UP000006731};
RN   [1] {ECO:0000313|EMBL:CAH09061.1, ECO:0000313|Proteomes:UP000006731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC   Onslow {ECO:0000313|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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DR   EMBL; CR626927; CAH09061.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5LA14; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   PaxDb; 272559-BF9343_3280; -.
DR   KEGG; bfs:BF9343_3280; -.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_009520_1_1_10; -.
DR   Proteomes; UP000006731; Chromosome.
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; cd16894; MltD-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
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; PF01464; SLT; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006731}.
FT   DOMAIN          51..149
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   271 AA;  31428 MW;  C9D2FF0F98BDB855 CRC64;
     MFDGDTIDLR RYDRRERMDR ELMSFTYMHS STMQMIKRAN RYFPVIEPLL KANGIPDDFK
     YLMVIESNLN PIARSPAGAA GLWQFMPVTA REFGLEVNDN VDERYHIEKA TAAACRYFKQ
     AYAKYGDWMA VSASYNAGQG RISSQLDKQL ADHAMDLWLA EETSRYMFRL LAVKEVFGNP
     QRFGFLLKRE HLYPAIPYKE VAVDTEISDL SNFAQKQGIT YAQLRDANPW LRGSSLKNKT
     GKKYVLHIPT QEGMNYDSRK TVPHEHKWVI D
//
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