ID A3V4T6_9RHOB Unreviewed; 719 AA.
AC A3V4T6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SKA53_13941 {ECO:0000313|EMBL:EAQ06654.1};
OS Yoonia vestfoldensis SKA53.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ06654.1, ECO:0000313|Proteomes:UP000004507};
RN [1] {ECO:0000313|EMBL:EAQ06654.1, ECO:0000313|Proteomes:UP000004507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ06654.1,
RC ECO:0000313|Proteomes:UP000004507};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) 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}.
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:EAQ06654.1}.
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DR EMBL; AAMS01000004; EAQ06654.1; -; Genomic_DNA.
DR RefSeq; WP_007206727.1; NZ_CH672414.1.
DR AlphaFoldDB; A3V4T6; -.
DR STRING; 314232.SKA53_13941; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_5; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000004507; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000004507};
KW Transferase {ECO:0000313|EMBL:EAQ06654.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 126..309
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 397..636
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 77577 MW; D0602A4E6534D4FD CRC64;
MSSNGKRRTP LVADKRYQGK ATPKKPAAKK PAPARKPRTR KTARRGRPTT LLGWLFWPFR
ILLRIIWAIS WRAGLVAALI ITGVSIYFAQ QMPPVQTLID QRARGSVTMA DLTGEVFAWR
GDQFGGMVTA RTVSPHLHNA VIAVEDRRFY AHFGLSPRGI ASAIRINLSE GRGPLSGNGG
STITQQTAKL LCLGVPYESS AWESEADYEA DCRRTTLARK VREAFYAMGM EIAYTKEEIL
TLYLNRAYLG AGSRGFEAAA QRYFGISAAE VNPAQAAMLA GLLKAPSTLA PTANIERSRE
RAAVVVRLME GQGYLTAAQA QEAITNPAAL SRAAEARSGG FFADWVMESG PEFFTRNTTE
DVIIRTTLDQ RIQRAAEEAL VSVFENLVAD GSEAQAAIVV MSADGAVRAM VGGRNLRATG
AFNRATQALR QTGSAFKPFI YAAALDLGVS PYAMVDDAPQ CWSIRGSREW CPENYDREFK
GPVTLTQALA ESRNLPAIVL SEDVGREYVR NVANGFGLQG ELAEGPALAL GVSESTLLNI
TGAYAGILNG GSQVTPYGLL DLRIQGDPAV LMDSQGVGIG NRIISEQAAR QLTWMMTRVV
EEGTGRRARI DGWEIAAKTG TTNSARDAWF IGFTGDYVTG VWMGYDNNTP LSGVTGGGLP
AEIWRETMVR VLEGRMPTPL PMTMPQTAAP AGILESQGGE VVDDDIVNLL DLLVGGEAN
//
