ID J2KZM3_9BURK Unreviewed; 818 AA.
AC J2KZM3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=PMI15_04327 {ECO:0000313|EMBL:EJL78478.1};
OS Polaromonas sp. CF318.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1144318 {ECO:0000313|EMBL:EJL78478.1, ECO:0000313|Proteomes:UP000007275};
RN [1] {ECO:0000313|EMBL:EJL78478.1, ECO:0000313|Proteomes:UP000007275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF318 {ECO:0000313|EMBL:EJL78478.1,
RC ECO:0000313|Proteomes:UP000007275};
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:EJL78478.1}.
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DR EMBL; AKIV01000138; EJL78478.1; -; Genomic_DNA.
DR AlphaFoldDB; J2KZM3; -.
DR PATRIC; fig|1144318.3.peg.4171; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007275; Unassembled WGS sequence.
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: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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 ECO:0000313|EMBL:EJL78478.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..255
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 412..650
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 818 AA; 88875 MW; B95945D5BABA91AD CRC64;
MKNPFQTFFQ APLGPRLRAF AASIPGRLRK LTKRDVALAL AAIPAMLLLY TVLLLPFTPS
ISDLLKAKTA KPSVLMSVDG QELASFQRAN RGWVKLDAIS PNVVAALIAT EDHRFYEHHG
MDFRRTVSSV LLTLTGRKQG GSTLTQQLAR NMYPEEIGRS ATLTRKLKEA ITAFKIEAVY
SKDEILESYL NTVPFLYNAY GIEMAARTYF DKSASELDVL QSATLVGMLK GASYYNPVVN
PDRALQRRNI VLMQMVKHGK LPEAKLAALK KKPLKIDFER LDPELGEMPH LAQQLRRWLI
EWADRNDYNI YADGLVVRTT IDSRLQAMAN KALVAQGDRL QKVVAGDWRF NSGWKAKSGA
QRELALAFVR DTAEYKAARA AGQPDEQALK TLLANAAFMQ TLKDEKTRLQ AGFMALDPTN
GQVRAWVGSR DFSDDQFDHV QQARRQPGST FKPFVYGAAF EEGARQSDGF VDGVVEIPLG
NGAFWRPTDG GGPSGEFMSL RQGLMFSKNT ITAQVMQVVG PAHVAKLARA MGVRQSKLEE
VPSLALGTSP VTLKEMVTAY GTLANDGRYI EPIIVTRVED RNGKVLEQFE AKAPETVMSA
TVAQTLLDVM RGVIDQGTGA AIRSRYGLRA DLAGKTGTTQ GNTDGWFVMM HPQLVAGAWV
GFNDNRVTMG DSWGQGARSA LPIVGEFFQQ AIKAKVVDAE QRFPAPQGGG VTDQEQQRVE
ALLNGAEPPQ EGQPGELPAG VGMAGASTGG QGGAPRWQPA PVIKYVTIQA PAENQVPAVQ
GGDSGGMPGV VLQPVTPVPV EKLPVFPGVV VGPPIAPR
//
