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Database: UniProt
Entry: A0A501WYC7_9RHOB
LinkDB: A0A501WYC7_9RHOB
Original site: A0A501WYC7_9RHOB 
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
//
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