ID F2JY07_MARM1 Unreviewed; 373 AA.
AC F2JY07;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 OrderedLocusNames=Marme_1476 {ECO:0000313|EMBL:ADZ90743.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ90743.1, ECO:0000313|Proteomes:UP000001062};
RN [1] {ECO:0000313|EMBL:ADZ90743.1, ECO:0000313|Proteomes:UP000001062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC {ECO:0000313|Proteomes:UP000001062};
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
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}.
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DR EMBL; CP002583; ADZ90743.1; -; Genomic_DNA.
DR AlphaFoldDB; F2JY07; -.
DR STRING; 717774.Marme_1476; -.
DR KEGG; mme:Marme_1476; -.
DR PATRIC; fig|717774.3.peg.1532; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_2_2_6; -.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001062; Chromosome.
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:UP000001062};
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 25..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 279..300
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 312..339
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ SEQUENCE 373 AA; 40742 MW; E8D4B52902982E30 CRC64;
MNATWYQRFI RFTNARLWRL THIDVLLAAS LVLLMSGGLV VLYSASGQNM EMVERQVFRL
ALGFAVCLAL AQLPPKYMLR ASPLLFVAIA GLLVGVLLFG VGAKGAQRWL EIPGGPRFQP
SEIMKIVMPM MIAWYFAHRP LPPSFKQIAT VLVIIVIPVL MIAKQPDLGT SLLVAVSGLF
VLFLAGLPWI YMLSAGACAP VAGYLLWHVM HDYQRQRVLT FLNPESDPLG SGWNIIQSKT
AIGSGGVYGK GWLEGTQAQL NFLPESHTDF IIAVLGEEFG MLGCGVLIFA YLLVIARGLY
ISATAEDNYA RLLAGSLTLT FFVYMFVNIG MVSGILPVVG VPLPLVSYGG TSIITIMATF
GILMSIQTHK RAR
//
