ID C0RHT3_BRUMB Unreviewed; 718 AA.
AC C0RHT3;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=BMEA_A0622 {ECO:0000313|EMBL:ACO00391.1};
OS Brucella melitensis biotype 2 (strain ATCC 23457).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=546272 {ECO:0000313|EMBL:ACO00391.1, ECO:0000313|Proteomes:UP000001748};
RN [1] {ECO:0000313|Proteomes:UP000001748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23457 {ECO:0000313|Proteomes:UP000001748};
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Han C., Detter J.C., Bruce D., Brettin T.S.;
RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL Submitted (MAR-2009) 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; CP001488; ACO00391.1; -; Genomic_DNA.
DR AlphaFoldDB; C0RHT3; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; bmi:BMEA_A0622; -.
DR HOGENOM; CLU_006354_2_7_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001748; Chromosome I.
DR GO; GO:0016020; C:membrane; 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; 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 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 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..285
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 373..607
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 654..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 79756 MW; 463FBCAD15BA9192 CRC64;
MRNTAEKDRG NDKRKPFRVS RLIGLDAWID SALYNLHFRL GEWWENITIF SRRFRVRGFR
RFTVEVLDEG FTLGVAGSVL MLMLALPAFE ETKKDWRAQD DYAVTFLDRY GNEIGRRGIL
HRQAVPIDEL PDHVIKAVLG TEDRRFFDHY GIDLMGLSRA LSQNMRANGV VQGGSTITQQ
LAKNLFLSNE RTIERKVKEA FLALWLESNL SKKEILQLYL DRAYMGGGTF GIAAASEFYF
GKNVKDISLA EAAMLAGLFK APAKFAPHVN LPAARARANV VLSNMVESGF LSEGQVAVAR
RHPASVIDRA KDESPDYFLD WAFDEVKKVA DRFNQHTLIV RTTLDRNIQK AAEESLEFHL
RQYGKEYNVS EAATVVLAND GSVRALVGGR DYGESQFNRA TRALRQAGSS FKPYVYAAAM
EKGLTPSTIV SDAPISWGNW SPRNYGRSFA GRVDLTTALV RSLNSVPVRL ARDYLTTAPV
VALTKAMGVE SHISSHKTMV LGTSEMTVMD QATGFNVFAN AGMAGNRHAF TQILASDGKV
LWDFGRDAPK PHRALSEKAA LEMNSMLVQV PERGTGRRAA LTMTRVAGKT GTTQNYRDAW
FVGFTGNFTA AVWFGNDNFT PMKELTGGVL PAMAWQRMMA YAHQNIELKP LPGVNPPFPA
QPKNPPAQVA DTRPHETMAA PPRVLSPLAT KILKELHDRF LAAPPLPTIA ERTKVSVL
//
