ID U3AVW3_9VIBR Unreviewed; 373 AA.
AC U3AVW3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Peptidoglycan glycosyltransferase MrdB {ECO:0000256|HAMAP-Rule:MF_02079};
DE Short=PGT {ECO:0000256|HAMAP-Rule:MF_02079};
DE EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_02079};
DE AltName: Full=Cell elongation protein RodA {ECO:0000256|HAMAP-Rule:MF_02079};
DE AltName: Full=Cell wall polymerase {ECO:0000256|HAMAP-Rule:MF_02079};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000256|HAMAP-Rule:MF_02079};
DE Short=PG polymerase {ECO:0000256|HAMAP-Rule:MF_02079};
GN Name=mrdB {ECO:0000256|HAMAP-Rule:MF_02079,
GN ECO:0000313|EMBL:GAD77362.1};
GN Synonyms=rodA {ECO:0000256|HAMAP-Rule:MF_02079};
GN ORFNames=VAZ01S_072_00260 {ECO:0000313|EMBL:GAD77362.1};
OS Vibrio azureus NBRC 104587.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219077 {ECO:0000313|EMBL:GAD77362.1, ECO:0000313|Proteomes:UP000016567};
RN [1] {ECO:0000313|EMBL:GAD77362.1, ECO:0000313|Proteomes:UP000016567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104587 {ECO:0000313|EMBL:GAD77362.1,
RC ECO:0000313|Proteomes:UP000016567};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio azureus NBRC 104587.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell wall
CC elongation. {ECO:0000256|HAMAP-Rule:MF_02079}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02079};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02079}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02079}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02079}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SEDS family. MrdB/RodA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02079}.
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:GAD77362.1}.
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DR EMBL; BATL01000072; GAD77362.1; -; Genomic_DNA.
DR RefSeq; WP_021711101.1; NZ_BATL01000072.1.
DR AlphaFoldDB; U3AVW3; -.
DR STRING; 1219077.VAZ01S_072_00260; -.
DR eggNOG; COG0772; Bacteria.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000016567; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR HAMAP; MF_02079; PGT_RodA; 1.
DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR InterPro; IPR001182; FtsW/RodA.
DR InterPro; IPR011923; RodA/MrdB.
DR NCBIfam; TIGR02210; rodA_shape; 1.
DR PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR PANTHER; PTHR30474:SF1; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE MRDB; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02079};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02079};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02079};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02079};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_02079};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02079};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02079};
KW Reference proteome {ECO:0000313|Proteomes:UP000016567};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02079};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02079};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02079}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 163..180
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 187..205
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 275..296
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 308..335
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 341..362
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ SEQUENCE 373 AA; 40606 MW; D4A5D5BD10DD148A CRC64;
MKMDPSTGKN RSLFERFHID LPLLLGILAL MGFGLVIMYS ASGQNLAMMD RQAARMGLSL
LVMIVLAQLS PRSYEGVAPL MFIAGIVLLL GVLFFGEASK GAQRWLNLGF VRFQPSELLK
LAVPLMVARY IGRQPLPPTF RTLIVALILV CLPTILIAKQ PDLGTSILIA ASGIFVIFLA
GISWKIIIAA ALALGGFIPI LWFFLMREYQ KVRVRTLFNP ESDPLGAGYH IIQSKIAIGS
GGISGKGWLQ GTQSQLEFLP ERHTDFIFAV IAEEWGMIGF LGLLSIYLFI IGRGLYLASQ
AQTAFGRMMA GSIVLSFFVY IFVNIGMVSG ILPVVGVPLP LISYGGTSMV TLMAGFGILM
SIHTHRKAFS KAT
//
