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Database: UniProt
Entry: H6RRR5_BLASD
LinkDB: H6RRR5_BLASD
Original site: H6RRR5_BLASD 
ID   H6RRR5_BLASD            Unreviewed;       363 AA.
AC   H6RRR5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Transglycosylase domain protein {ECO:0000313|EMBL:CCG01708.1};
DE            EC=3.2.-.- {ECO:0000313|EMBL:CCG01708.1};
GN   OrderedLocusNames=BLASA_0755 {ECO:0000313|EMBL:CCG01708.1};
OS   Blastococcus saxobsidens (strain DD2).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG01708.1, ECO:0000313|Proteomes:UP000007517};
RN   [1] {ECO:0000313|EMBL:CCG01708.1, ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|EMBL:CCG01708.1,
RC   ECO:0000313|Proteomes:UP000007517};
RX   PubMed=22535935; DOI=10.1128/JB.00320-12;
RA   Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA   Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA   Gury J., Pujic P., Normand P.;
RT   "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT   Bacterium.";
RL   J. Bacteriol. 194:2752-2753(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA   Genoscope.;
RT   "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC       {ECO:0000256|ARBA:ARBA00010830}.
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DR   EMBL; FO117623; CCG01708.1; -; Genomic_DNA.
DR   RefSeq; WP_014374618.1; NC_016943.1.
DR   AlphaFoldDB; H6RRR5; -.
DR   STRING; 1146883.BLASA_0755; -.
DR   KEGG; bsd:BLASA_0755; -.
DR   eggNOG; COG3583; Bacteria.
DR   HOGENOM; CLU_036884_1_1_11; -.
DR   OrthoDB; 1404170at2; -.
DR   Proteomes; UP000007517; Chromosome.
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; cd13925; RPF; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR   InterPro; IPR007137; DUF348.
DR   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR010618; RPF.
DR   PANTHER; PTHR39160; CELL WALL-BINDING PROTEIN YOCH; 1.
DR   PANTHER; PTHR39160:SF4; RESUSCITATION-PROMOTING FACTOR RPFB; 1.
DR   Pfam; PF03990; DUF348; 3.
DR   Pfam; PF07501; G5; 1.
DR   Pfam; PF06737; Transglycosylas; 1.
DR   SMART; SM01208; G5; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51109; G5; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:CCG01708.1};
KW   Hydrolase {ECO:0000313|EMBL:CCG01708.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007517};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          196..276
FT                   /note="G5"
FT                   /evidence="ECO:0000259|PROSITE:PS51109"
SQ   SEQUENCE   363 AA;  38415 MW;  93C985FF1A024F14 CRC64;
     MRRSLQLSLF ALVLVGLVGG TLAFFLAQKS VALTVDGQTR DVGTYAGTVG EVLEEEGLTL
     AAHDVVLPAT DHALSDGDAV VLNRARPLEL TVDGVSREVH VTALSVEEAL DQLGFRTDGL
     VLSASRAERL PLEGMQLTIT TPKDVVLVAD GQERVVTTAA ATAGDLLAEQ GIALSETDRT
     SLYLEQGLLN RMRLQVYRVQ VSEVTETAPI AHGRVETANA EAFEGDDEVT QQGVDGEQAT
     TYRVTVVDGQ ETSREQLSST VTRAPVDEQV TVGTKARPAN SPTADGLNWA ALAACESGGR
     PDAVSSTGKY RGMYQFSQAT WNGVGGTGDP AAASADEQTY RAQLLYNRSG AGQWPHCGPR
     LFG
//
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