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Database: UniProt
Entry: Q2YRM1_BRUA2
LinkDB: Q2YRM1_BRUA2
Original site: Q2YRM1_BRUA2 
ID   Q2YRM1_BRUA2            Unreviewed;       267 AA.
AC   Q2YRM1;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=SLT domain {ECO:0000313|EMBL:CAJ11487.1};
DE            EC=3.2.1.- {ECO:0000313|EMBL:CAJ11487.1};
GN   OrderedLocusNames=BAB1_1531 {ECO:0000313|EMBL:CAJ11487.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ11487.1, ECO:0000313|Proteomes:UP000002719};
RN   [1] {ECO:0000313|EMBL:CAJ11487.1, ECO:0000313|Proteomes:UP000002719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308 {ECO:0000313|EMBL:CAJ11487.1,
RC   ECO:0000313|Proteomes:UP000002719};
RX   PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG   Microbial Genomics Group;
RG   Lawrence Livermore National Laboratory;
RG   and the Genome Analysis Group;
RG   Oak Ridge National Laboratory;
RA   Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
CC   -!- SIMILARITY: Belongs to the virb1 family.
CC       {ECO:0000256|ARBA:ARBA00009387}.
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DR   EMBL; AM040264; CAJ11487.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2YRM1; -.
DR   STRING; 359391.BAB1_1531; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   KEGG; bmf:BAB1_1531; -.
DR   PATRIC; fig|359391.11.peg.978; -.
DR   HOGENOM; CLU_1040800_0_0_5; -.
DR   PhylomeDB; Q2YRM1; -.
DR   Proteomes; UP000002719; Chromosome I.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:CAJ11487.1};
KW   Hydrolase {ECO:0000313|EMBL:CAJ11487.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002719};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..267
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004219307"
FT   DOMAIN          56..154
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   267 AA;  28145 MW;  3955FE868C5AA3BF CRC64;
     MNQFIMTIAV LAVASILHAA VGVFAAFAAD EPAPPIHAPS LSPDKPAPTV NRICQLIEAN
     AEAHGIPKDF FARLIWKESR FDHNAVSPVG AQGIAQFMPY TAKERGLVDP FDVEQAIPAS
     AGFLRDLKDA FGNWGLAAAA YNAGAGRVSS WMRTGGFLPL ETEDYVLDIT GAPADDFAAG
     QEVVNRPLDP KLGFHDACRS SALQRSPCHG SSRNLGAYSS PEISAAASPS TNGTDYASNL
     PPFLQGTIRL SAAFARQSAG AESMRCA
//
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