ID C1DQU0_AZOVD Unreviewed; 1029 AA.
AC C1DQU0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=Avin_13960 {ECO:0000313|EMBL:ACO77613.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO77613.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO77613.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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}.
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DR EMBL; CP001157; ACO77613.1; -; Genomic_DNA.
DR RefSeq; WP_012700032.1; NC_012560.1.
DR AlphaFoldDB; C1DQU0; -.
DR STRING; 322710.Avin_13960; -.
DR EnsemblBacteria; ACO77613; ACO77613; Avin_13960.
DR KEGG; avn:Avin_13960; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_012369_0_0_6; -.
DR OrthoDB; 8552189at2; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transferase {ECO:0000313|EMBL:ACO77613.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..350
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
SQ SEQUENCE 1029 AA; 115293 MW; 2F376A7AEF638495 CRC64;
MGVIWQRDEQ RSALSERDLP TSAPPPSHRL RWRLLVWFVV LAGAAVLGVL LYFELQTSRL
QSRELSRYAA TLGYSVGDGP SPAIHFPEYG PYDRRLGYTA LPEWLPRLEQ RGFEITRQAR
FSQPLLEYSH RRLFPPYAEK PQAGLTISDC RGMPLYSYRL PREFYSSYAS IPPLVVHSLL
FIENRYLLDP SQPLANPAVD WPRFAKAALS QVREMFGLSG QTAGGSTLAT QIEKYRHSPD
GLTDSAMEKL RQMFSASVRA YQGGAQTMEA RRNVVRDYLN SVPLAAAPGY GEVHGLADGL
RVWYGTDFAQ VNRLLASADA DPAERGLALR QVLSLLIAQR RPSHYLIAGR EELATLTDSH
IRLLRKGGLL DPVLAEAALA RRAVFRDWMQ EPVVQPVETT KGISVARSRL ATLLQRSLYD
LDRFDLSAST PLQGELQDAV TRYLGQLADP SFAEGIGLFG ERLLSPEKTA EVRYSFTLFE
RSGDSFLVRV QTDSTTQPFD INEGSKLELG STAKLRVLTT YLEIIAELHA RFAGQERTAL
QAARAETEPL DFLTQWAIEW LMANPGGTLP AMLDAALERR YSASPGESFF TGGGLHTFTN
FNRVDNGRRP TMREALRDSI NLPFVRLLRD IVRYTIYQSP NNSVALLKDD QDPRRLEYLT
RFADREGTVY LRRFWNKYRG KSSDERLATF LEGLRVTSVR LAAVHRYLLP QSDRATFDTF
LRAHLPNDRT LTEKRLDSLY RSYGPGAYSL PDQGYIARVH PLDLWLLGYL IQHPAASYQE
VVEASRDERQ EVYGWLFKSR HRSARDSRIR TMVEVEAFLD IHQRWQQLGY PFPHLVPSLA
TALGSSGDRP AALAELIGII LNDGVRLPVV RIDNLEFAVD TPYETRLGLA PGRARRVLAP
EVAAALRGAL AQVVENGTAR RLFGSFQQAD GKPLTVGGKT GTGDNRIQRV ARGGYVISSQ
ALNRTATFVF YLGPNHFGTL TAYVPGRAAE KFRFTSALPV QVLKGMAPIL QPYLRGQNSL
CQAPASARN
//
