ID J3C713_9BURK Unreviewed; 732 AA.
AC J3C713;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=PMI40_03694 {ECO:0000313|EMBL:EJM99808.1};
OS Herbaspirillum sp. YR522.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJM99808.1, ECO:0000313|Proteomes:UP000007507};
RN [1] {ECO:0000313|EMBL:EJM99808.1, ECO:0000313|Proteomes:UP000007507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR522 {ECO:0000313|EMBL:EJM99808.1,
RC ECO:0000313|Proteomes:UP000007507};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJM99808.1}.
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DR EMBL; AKJA01000120; EJM99808.1; -; Genomic_DNA.
DR RefSeq; WP_008117870.1; NZ_AKJA01000120.1.
DR AlphaFoldDB; J3C713; -.
DR STRING; 1144342.PMI40_03694; -.
DR PATRIC; fig|1144342.3.peg.3425; -.
DR eggNOG; COG4953; Bacteria.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007507; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007507};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..732
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003764379"
FT DOMAIN 54..220
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 304..543
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 632..716
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 732 AA; 79935 MW; 8ACF678C4730CFE1 CRC64;
MIRPLPAALL AAALLGPPAA QAAPGFAEVK RDFVPSEASL LDRHGELLQR QRVDMDQRKL
SWVSLEDVSP AMRRSLVASE DRRFYQHSGI DWNAVAASAW GNLWHSRTRG ASTITMQLAG
LLHDDLRRKS NARSLSQKLS QAWVAQGLER SWRKDQILEA YLNLVAFRGE LVGVHALSRV
MFGKHPSGLN ESEAAVAVAL IRGPNATPRR VAERACAILK DEGVPEQCQG LEGRTELYLA
RATARRDLPG ASDAPQLAPH LARKLLERPG QQLRSTLDAP LQRFANQALR RQLSGLVERN
IEDGAVIVID NASGEVLAWV GSSGSLSGAA DVDGVVAQRQ AGSTLKPFLY EQAIENRWLT
AASLLDDSPV NLATTAGLYV PQNYDKQFKG LVSLRTALGS SLNIPAVRTL VMVTPERFFQ
RLQALGFNLR ENGDYYGYSL ALGSADVTLA NLANAYRALA NQGRYSPLRT RLEQGGAVRP
VQVMNPEASF IVGDILSDRS ARARTFGLEN ALATRMWSAV KTGTSKDMRD NWCVGYSTRY
TVGVWVGNAS GAPMWDVSGV TGAAPVWQEV MQYLHSARGT PMKVAVPGTP AGVVARTIHY
QDQIEASRTE YFLPGTAQDD IRVARGADIR TAIAYPTAGM LSALDPDIPP QRQRIRFRAQ
GVPAGSRWVL DGKTIPESMR VQGSRDELLA DWMPWPGRHL LVLQDSAGAQ LDSVRFEVRG
AVERAQVEPA RK
//
