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Database: UniProt
Entry: H0TLS8_9BRAD
LinkDB: H0TLS8_9BRAD
Original site: H0TLS8_9BRAD 
ID   H0TLS8_9BRAD            Unreviewed;       183 AA.
AC   H0TLS8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Endolytic peptidoglycan transglycosylase RlpA {ECO:0000256|HAMAP-Rule:MF_02071};
DE            EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02071};
GN   Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN   ORFNames=BRAS3843_2110004 {ECO:0000313|EMBL:CCE07416.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE07416.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
CC   -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC       glycan strands that lack stem peptides. {ECO:0000256|HAMAP-
CC       Rule:MF_02071}.
CC   -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_02071, ECO:0000256|RuleBase:RU003495}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCE07416.1}.
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DR   EMBL; CAFK01000126; CCE07416.1; -; Genomic_DNA.
DR   RefSeq; WP_008969933.1; NZ_CAFK01000126.1.
DR   AlphaFoldDB; H0TLS8; -.
DR   OrthoDB; 9779128at2; -.
DR   Proteomes; UP000002686; Unassembled WGS sequence.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd22268; DPBB_RlpA-like; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   HAMAP; MF_02071; RlpA; 1.
DR   InterPro; IPR034718; RlpA.
DR   InterPro; IPR009009; RlpA-like_DPBB.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   InterPro; IPR012997; RplA.
DR   NCBIfam; TIGR00413; rlpA; 1.
DR   PANTHER; PTHR34183; -; 1.
DR   PANTHER; PTHR34183:SF8; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
DR   Pfam; PF03330; DPBB_1; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02071};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002686}.
FT   DOMAIN          93..178
FT                   /note="RlpA-like protein double-psi beta-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF03330"
FT   REGION          41..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   183 AA;  19049 MW;  796500CCED67EFB6 CRC64;
     MLKLNNLPVA KIAGSRTALA VAVALIVGGT ATEASARARH HHHRYHHHHA ARHMGEAASE
     QASNGWSSNG WSNGSWMNAN ASFGSSSGGG RTFSGMASYY GSESGSRTAS GQRMNSNAMT
     CAHRSLPFGT KLRVTHGGQS VIVTVNDRGP FIRGRVLDLS TGAARAIGLT RAGVGRVTAE
     VVS
//
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