ID A0A501WYC7_9RHOB Unreviewed; 379 AA.
AC A0A501WYC7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=rodA {ECO:0000256|HAMAP-Rule:MF_02079,
GN ECO:0000313|EMBL:TPE53590.1};
GN Synonyms=mrdB {ECO:0000256|HAMAP-Rule:MF_02079};
GN ORFNames=FJM51_00630 {ECO:0000313|EMBL:TPE53590.1};
OS Amaricoccus solimangrovi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Amaricoccus.
OX NCBI_TaxID=2589815 {ECO:0000313|EMBL:TPE53590.1, ECO:0000313|Proteomes:UP000319255};
RN [1] {ECO:0000313|EMBL:TPE53590.1, ECO:0000313|Proteomes:UP000319255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB172011 {ECO:0000313|EMBL:TPE53590.1,
RC ECO:0000313|Proteomes:UP000319255};
RA Huang H., Mo K., Hu Y.;
RT "A novel bacterium of genus Amaricoccus, isolated from marine sediment.";
RL Submitted (JUN-2019) 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:TPE53590.1}.
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DR EMBL; VFRP01000001; TPE53590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A501WYC7; -.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000319255; 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:UP000319255};
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 53..74
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 105..131
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 143..159
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 171..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 349..367
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ SEQUENCE 379 AA; 40601 MW; FD2F3F40B638F230 CRC64;
MSARGTGAPR GAAKLLAVHW PLVLLLSAVA GMGFMMLYSV AGGSLDPWAR AQMIRFALGL
CVMLVIAMID IRFWKLVSPL AYLGSFALLL YVEAAGHVGM GAQRWINLGF IVLQPSEMMK
ISLVMVLAAY YARLDPGKVS RPLWMVPPLA LILAPVALVM TQPDLGTSIM LLAGGAAVMF
LAGVSIWYFA TAAAAAAGLV TLVLRSRGTD WQLLRDYQFN RIDTFLDPGR DPLGTGYHIT
QAKIALGSGG LAGRGFMQGT QSRLNFLPEK HTDFIFTTLA EEFGFLGTLA LLILFTLVIL
FCVQSAIANR DRFGALLTGG IGATFFLFFA VNMAMVMGLM PVVGVPLPLV SYGGSAMLVL
LAAFGLAQSA HVHRPRERG
//