ID A0A0H3C791_CAUVN Unreviewed; 536 AA.
AC A0A0H3C791;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Soluble lytic murein transglycosylase SdpB {ECO:0000313|EMBL:ACL94858.2};
DE EC=3.2.1.- {ECO:0000313|EMBL:ACL94858.2};
GN Name=sdpB {ECO:0000313|EMBL:ACL94858.2};
GN OrderedLocusNames=CCNA_01393 {ECO:0000313|EMBL:ACL94858.2};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL94858.2, ECO:0000313|Proteomes:UP000001364};
RN [1] {ECO:0000313|EMBL:ACL94858.2, ECO:0000313|Proteomes:UP000001364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX PubMed=20472802; DOI=10.1128/JB.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL94858.2; -; Genomic_DNA.
DR RefSeq; WP_024265701.1; NC_011916.1.
DR RefSeq; YP_002516766.2; NC_011916.1.
DR AlphaFoldDB; A0A0H3C791; -.
DR GeneID; 7331851; -.
DR KEGG; ccs:CCNA_01393; -.
DR PATRIC; fig|565050.3.peg.1379; -.
DR HOGENOM; CLU_020668_0_0_5; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000001364; Chromosome.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR011990; TPR-like_helical_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; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:ACL94858.2};
KW Hydrolase {ECO:0000313|EMBL:ACL94858.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..536
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002605974"
FT DOMAIN 360..460
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 536 AA; 57963 MW; CD9D2CF822734176 CRC64;
MLLQLWARLL AVFSAFVLSA TALAAHASGL EPLSPDDVRY YRAAFTATDR GDFDSAEAAF
ANTRDRSLAG RLVFAKIMHP TRYSASYAEL TRWLDSHGEE AGADRVYSLA LKRKPNSKRA
AAPPVPTLFV ADESGPPPAD KGRAAREAYY SGDVKEALAL AIAGGERWIA GLSAYRLGDA
AQAQRFFEQV ADDAHEDEWL RAAGAFWAAR AASRQGDGGQ ARDLLLKAAH APHTFYGMIA
ARQLNLAGVP VTEPQEDAIA TLISRAAYVG PDTESLNALV TADPRARRAA ALAQIGRWRE
AGEELRAGLS LAETESLRAD WTTLALALNA KAPLNAGRPV RRVGGEDYPL PPLDPIGGFT
IDKAMVYALV RQESRFDPLA VSNAGAVGLM QVRPTSAADV VGDDKLRTDN TPLFDPAFNL
RAGQDYFTWL MDRGLKSPDV LRAVAAYNGG PATLNRTLAQ LGADCDSLLL IESLPFKETR
NYVEKVMASY WTYRQLMGAE NKTLDAVASG ARTVDFRLDP QVQMPTTIDQ LMAQLP
//
