ID Q9A3C7_CAUVC Unreviewed; 733 AA.
AC Q9A3C7;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=CC_3277 {ECO:0000313|EMBL:AAK25239.1};
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650 {ECO:0000313|EMBL:AAK25239.1, ECO:0000313|Proteomes:UP000001816};
RN [1] {ECO:0000313|EMBL:AAK25239.1, ECO:0000313|Proteomes:UP000001816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15 {ECO:0000313|Proteomes:UP000001816};
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R., Ohta N., Maddock J.R., Potocka I.,
RA Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T.,
RA Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J.,
RA Craven M.B., Khouri H., Shetty J., Berry K., Utterback T., Tran K.,
RA Wolf A., Vamathevan J., Ermolaeva M., White O., Salzberg S.L., Venter J.C.,
RA Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK25239.1; -; Genomic_DNA.
DR PIR; C87655; C87655.
DR RefSeq; NP_422071.1; NC_002696.2.
DR RefSeq; WP_010921109.1; NC_002696.2.
DR AlphaFoldDB; Q9A3C7; -.
DR SMR; Q9A3C7; -.
DR IntAct; Q9A3C7; 2.
DR MINT; Q9A3C7; -.
DR STRING; 190650.CC_3277; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAK25239; AAK25239; CC_3277.
DR KEGG; ccr:CC_3277; -.
DR PATRIC; fig|190650.5.peg.3283; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_4_5; -.
DR BioCyc; CAULO:CC3277-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001816; Chromosome.
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; IPR031375; PBP_N.
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; PF17093; PBP_N; 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 Reference proteome {ECO:0000313|Proteomes:UP000001816};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 84..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..138
FT /note="Penicillin-binding protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17093"
FT DOMAIN 140..314
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 409..637
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 80089 MW; D7F31A03BF19C7BF CRC64;
MNDWTLPPYK FDDGKSPGEP PKPGPASASD GVSQDPWAPQ GPDPFRLSSD AATPPPPPEP
PPEEPFRADL KHAAAKKKAR KWGWVWGTLL VGFLLAVLSV AGGGAYVWFK YLKDTPALPS
REALFAVNRA PGIRFEDRNG QVIATRGPRY GQRITLGTVP NYVPMAFLAA EDRRFYQHGA
IDVQGIARAA WINWRAGKTR QGASTLTQQL AKGLFLTPDR VVKRKLQEML LAYKLEQILT
KDEILELYLN RIYFGAGTYG IDGASQTYFG KPASQLTLSE AALLASLPKA PSRLALTRDM
ERALARSRLI LANMRKEGWI TPEQESRALD DTPRLSPMAL QDEGDYGWVL DYATAEAVKI
AGQNAPDLVV RLTIDPLLQS EGAEVVRQTM ATETTRSGAS QAALLSLSAD GAIRAMVGGT
DYSESPFNRA VQAKRQPGST FKPFVYAAAV EKGVLPTDMR VDEPVKFGTW EPENYSGGYR
GPMTVEDALV TSINTVAVKL GQEVGGPAIG DLVRRFGITS LPPSPDLSVA LGSYEVNLLQ
ITSGFQVFQQ GGLRIEPYVI ESITTQGGQQ IFQHQPPQGE RRVYDVAHAS MMVKMMKKVV
TQGTAQRAAF GRPVAGKTGT SQNWRDAWFV GFTPDYVTGV WVGNDDEKPM NKVVGGDIPA
SIWRRFMMTA HQTLAVRDFE WLLPDPAPQS EPDPRNGFYE TLSAEFSRAA SELETTTPVA
PAPGQPPPDN LPY
//
