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Database: UniProt
Entry: A0A370DA14_9GAMM
LinkDB: A0A370DA14_9GAMM
Original site: A0A370DA14_9GAMM 
ID   A0A370DA14_9GAMM        Unreviewed;       352 AA.
AC   A0A370DA14;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   Synonyms=rodA {ECO:0000256|HAMAP-Rule:MF_02079};
GN   ORFNames=DIZ80_16270 {ECO:0000313|EMBL:RDH81729.1};
OS   endosymbiont of Galathealinum brachiosum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=2200906 {ECO:0000313|EMBL:RDH81729.1, ECO:0000313|Proteomes:UP000254266};
RN   [1] {ECO:0000313|EMBL:RDH81729.1, ECO:0000313|Proteomes:UP000254266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1464 {ECO:0000313|EMBL:RDH81729.1};
RX   PubMed=30022157;
RA   Li Y., Liles M.R., Halanych K.M.;
RT   "Endosymbiont genomes yield clues of tubeworm success.";
RL   ISME J. 0:0-0(2018).
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:RDH81729.1}.
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DR   EMBL; QFXC01000013; RDH81729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370DA14; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000254266; 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|ARBA:ARBA00023316,
KW   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|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_02079}; Reference proteome {ECO:0000313|Proteomes:UP000254266};
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        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        35..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        99..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        120..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        145..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        247..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        294..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        322..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ   SEQUENCE   352 AA;  38658 MW;  EBFD1695E57A318E CRC64;
     MDHVLLLGIG ILMLLGLVVL YSAGDESSAL MNRQLTRIGL AVFVMLIIAQ IPSSTLRFWS
     PWMYIAGVIL LVLVLVMGDM GKGAQRWLDL GFIRFQPSEM MKLVTPMMIA WYFAEKPLPP
     SWSTLGVAVV LILVPTFLIA RQPDLGTSLL IFAAGFFVLF LGGLSWRLMI GMSVLAASML
     PVLWHFMHDY QKSRVMTLLD PQRDPLGAGY HIIQSQIAIG SGGVYGRGWL NGSQSHLNFL
     PEQSTDFIFA VFAEEFGLLG GLLLLVLYGF IIIRGLMIAV QGQDTYARLL GGSLSLTFFV
     YLFVNVGMVS GILPVVGVPL PLISYGGTSM VTLMASFGML MSINSHRKLW SK
//
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