ID D7H2D6_BRUAO Unreviewed; 720 AA.
AC D7H2D6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BAYG_00896 {ECO:0000313|EMBL:EFH34479.1};
OS Brucella abortus bv. 5 str. B3196.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=520453 {ECO:0000313|EMBL:EFH34479.1, ECO:0000313|Proteomes:UP000005752};
RN [1] {ECO:0000313|EMBL:EFH34479.1, ECO:0000313|Proteomes:UP000005752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3196 {ECO:0000313|EMBL:EFH34479.1,
RC ECO:0000313|Proteomes:UP000005752};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ward D., Whatmore A.M., Perrett L.L., O'Callaghan D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Brucella abortus bv. 5 str. B3196.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; GG774511; EFH34479.1; -; Genomic_DNA.
DR AlphaFoldDB; D7H2D6; -.
DR HOGENOM; CLU_006354_2_7_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005752; Unassembled WGS sequence.
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; 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; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 123..287
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 375..609
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 656..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 79995 MW; DFD798539B012C0E CRC64;
MFMRNTAEKD RGNDKRKPFR VSRLIGLDAW IDSALYNLHF RLGEWWENIT IFSRRFRVRG
FRRFTVEVLD EGFTLGVAGS VLMLMLALPA FEETKKDWRA QDDYAVTFLD RYGNEIGRRG
ILHRQAVPID ELPDHVIKAV LGTEDRRFFD HYGIDLMGLS RALSQNMRAN GVVQGGSTIT
QQLAKNLFLS NERTIERKVK EAFLALWLES NLSKKEILQL YLDRAYMGGG TFGIAAASEF
YFGKNVKDIS LAEAAMLAGL FKAPAKFAPH VNLPAARARA NVVLSNMVES GFLSEGQVAV
ARRHPASVID RAKDESPDYF LDWAFDEVKK VADRFNQHTL IVRTTLDRNI QKAAEESLEF
HLRQYGKEYN VSEAATVVLA NDGSVRALVG GRDYGESQFN RATRALRQAG SSFKPYVYAA
AMEKGLTPST IVSDAPISWG NWSPRNYGRS FAGRVDLTTA LVRSLNSVPV RLARDYLTTA
PVVALTKAMG VESPISSHKT MVLGTSEMTV MDQATGFNVF ANAGMAGNRH AFTQILASDG
KVLWDFGRDA PKPHRALSEK AALEMNSMLV QVPERGTGRR AALTMTRVAG KTGTTQNYRD
AWFVGFTGNF TAAVWFGNDN FTPMKELTGG VLPAMAWQRM MAYAHQNIEL KPLPGVNPPF
PAQPKNPPAQ VADTRPHETM AAPPRVLSPL ATKILKELHD RFLAAPPLPT IAERTKVSVL
//
