ID F4QRB6_9CAUL Unreviewed; 604 AA.
AC F4QRB6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Transglycosylase SLT domain protein {ECO:0000313|EMBL:EGF90753.1};
GN ORFNames=ABI_37860 {ECO:0000313|EMBL:EGF90753.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF90753.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; GL883079; EGF90753.1; -; Genomic_DNA.
DR RefSeq; WP_006274567.1; NZ_GL883079.1.
DR AlphaFoldDB; F4QRB6; -.
DR STRING; 715226.ABI_37860; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_020668_0_0_5; -.
DR Proteomes; UP000006512; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd13401; Slt70-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR006311; TAT_signal.
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; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51318; TAT; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..604
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003314367"
FT DOMAIN 442..544
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 604 AA; 64865 MW; 5DF1AE6249662865 CRC64;
MTSNRQTLLR LLAGAAFMAL ASAAMAAPVM AQDFLKPDFA AQDPAPLTAA EAATPAADET
VAFNTTPLPY ALVAGQAQAP KQAVAQSLPL AAWDAQLYQA AFQMIEAGDF AGADEKLAQV
KDQRLMGYAR FNKLFHRKYT STYDELMAWL GDYGDQPMAM RVWGLAKRKK PDGAPDPAFP
SLMGAVPAGD VATNAGTAVR LNATGSLNAA PQANYNPGAP TGEDLTPKSA RSAYNNGQLE
QAVKLGKQIG DHWVVGLANW RLGRYEPAMA AFKFVASDPS QNAWSQSGGA YWAGRAALKV
GKKDEAEGYF KVAASFPFTF YGLVAEQRLG VTPAVALSKK GELPTFAGQS RTAMVAALDG
DFGWTASHPK AQRMNALIQV GRVGDAQDEL QAAVQTATSA EERDRWLALS SHTQIPVSQL
KRTDKLFDAS LYPIPDFAPT GGYTVPKALV FALARKESKF NPKAYSYSGA YGLLQLMPAT
AALVENDASF TAKPKQLLTP EVNLRVGQRY IQRLFDAKMV DGDLLRTLAA YNAGPRPVKD
AVDSLGPDAD SLLFLESIPV AQTRQYVEEV AANYWIYRQL MGQPTKTLTM AANDARIIDA
SADK
//
