ID V6EZJ7_MAGGM Unreviewed; 387 AA.
AC V6EZJ7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:CDK97648.1};
GN Synonyms=rodA {ECO:0000256|HAMAP-Rule:MF_02079};
GN OrderedLocusNames=MGMSRv2__0433 {ECO:0000313|EMBL:CDK97648.1};
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944 {ECO:0000313|EMBL:CDK97648.1, ECO:0000313|Proteomes:UP000018922};
RN [1] {ECO:0000313|EMBL:CDK97648.1, ECO:0000313|Proteomes:UP000018922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC {ECO:0000313|Proteomes:UP000018922};
RX PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:e00171-e00114(2014).
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; HG794546; CDK97648.1; -; Genomic_DNA.
DR AlphaFoldDB; V6EZJ7; -.
DR STRING; 1430440.MGMSRv2__0433; -.
DR KEGG; mgy:MGMSRv2__0433; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_2_1_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000018922; Chromosome I.
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:UP000018922};
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 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 151..167
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 173..190
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 317..344
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 350..373
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ SEQUENCE 387 AA; 42800 MW; AB190578D9F5A3AD CRC64;
MLRPTQRLSS RLNRTEMSWR EKIWQINWSL IAVLTAIASV GFLTLYSAAK GSLEPWAIKQ
MIRFAVGIGL MITVAVVDLR FWMRHAYILY AVSIVLLIAV DLKGTIGMGA QRWIDLGFIQ
LQPSEIMKIA MILTLARYFH GASVQDVGRP TFLIPPLLLV LLPVALVMKQ PDLGTAMMVL
MSSGAIFFMA GVRIWKFALL LAGGLGSIPV AWQFLHDYQK KRVIIFLNPD QDPLGAGYHI
TQSKIALGSG GLFGKGYMNG TQSGLNFLPE KQTDFIFTMY GEEWGLMGGL FLLGLYVLLT
AFGYAIAMRC RAQFGRLVAL GITTTFFLYF FINTAMVMGL VPVVGVPLPL ISYGGTAMLS
LLFGWGLVMS AYIHRDLPIG RRGGHDD
//
