ID B5ZTV7_RHILW Unreviewed; 763 AA.
AC B5ZTV7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Lectin-like protein BA14k {ECO:0000256|ARBA:ARBA00020552};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=Rleg2_0767 {ECO:0000313|EMBL:ACI54062.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI54062.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI54062.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI54062.1,
RC ECO:0000313|Proteomes:UP000008330};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
CC -!- FUNCTION: Has immunoglobulin-binding and hemagglutination properties,
CC and can bind to mannose. Essential for virulence. May be involved in
CC LPS biosynthesis or polysaccharide transport.
CC {ECO:0000256|ARBA:ARBA00025321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
CC -!- SIMILARITY: Belongs to the BA14k family.
CC {ECO:0000256|ARBA:ARBA00010270}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP001191; ACI54062.1; -; Genomic_DNA.
DR RefSeq; WP_012556945.1; NC_011369.1.
DR AlphaFoldDB; B5ZTV7; -.
DR STRING; 395492.Rleg2_0767; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; rlt:Rleg2_0767; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008330; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012413; BA14K.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF07886; BA14K; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..354
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 443..679
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 82034 MW; 238A39604FC7E51D CRC64;
MPNSPESSGE SVSSSSSDRE KTLDSAVQAD ALDSPGTQGE DPQPPHGSFE QTRRAARTLF
GAIRQDLQAS SALAKLKAAA LLLKTKLTRS GRPGVTSPHK WLPTAWVKSW RGIRDRRSKP
RENRRSASFI AGWRKFALGF TLLVCLLVGS VLVWALKDVP WSEIRDGTLK PVVVLETADG
APLVRQGPYQ GPYARYDQFP PHLIDAVLSI EDRRFMDHFG IDPRGIARAF WRNLEAGSVV
EGGSTITQQL IKLQYLDSDR TIKRKIQEVV IAFWLEWKLG KAEILTRYLN SVYLGAGATG
MPAAARIYFN KDIGALNLPE SAMLAGLLRA PSQWNPIDNF EGARQRTMVV LDAMAANGKI
TAPQAAEAKT SFASLHPTTP TPRSGSWFAD WISPQASEIA GASPGSTTVR TTLVPTLQQI
AERVVKKGLD GEGKTVGASQ AALVAMTPDG AVVAMVGGRD YKASQFNRAV TAMRQPGSTF
KLFVYYAALK AGLTLSDQVL DAPIDIDGWS PENSGGDYRG WVTLAEAFAR SLNAASVTLA
QEVGLDNVIA AARELGIDAP LANTPSLALG TSEVNLLNLT SAYASVQLGR APVKPWGIID
FQAAGQPQTF RVGLQSKPTV DLSPYQSDLL GLLQLVVERG TGRGADPGTF AAGKTGTSQN
NRDAWFVGFT EALVVGVWVG NDDDAPMKGV TGGALPAHIW RDFMREAMSK PTLDGVRSTE
AAVDGQGAPQ SCNITACSRS YRSFRPSDCT YQPYSGGRRL CEK
//
