RODA_HAEIN
ID RODA_HAEIN Reviewed; 371 AA.
AC P44468;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Peptidoglycan glycosyltransferase MrdB {ECO:0000255|HAMAP-Rule:MF_02079};
DE Short=PGT {ECO:0000255|HAMAP-Rule:MF_02079};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_02079};
DE AltName: Full=Cell elongation protein RodA {ECO:0000255|HAMAP-Rule:MF_02079};
DE AltName: Full=Cell wall polymerase {ECO:0000255|HAMAP-Rule:MF_02079};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000255|HAMAP-Rule:MF_02079};
DE Short=PG polymerase {ECO:0000255|HAMAP-Rule:MF_02079};
GN Name=mrdB {ECO:0000255|HAMAP-Rule:MF_02079}; Synonyms=rodA;
GN OrderedLocusNames=HI_0031;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell wall
CC elongation. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_02079};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02079}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02079}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02079}.
CC -!- SIMILARITY: Belongs to the SEDS family. MrdB/RodA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02079}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC21709.1; -; Genomic_DNA.
DR PIR; B64044; B64044.
DR RefSeq; NP_438204.1; NC_000907.1.
DR RefSeq; WP_005649852.1; NC_000907.1.
DR AlphaFoldDB; P44468; -.
DR SMR; P44468; -.
DR STRING; 71421.HI_0031; -.
DR EnsemblBacteria; AAC21709; AAC21709; HI_0031.
DR KEGG; hin:HI_0031; -.
DR PATRIC; fig|71421.8.peg.31; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_2_2_6; -.
DR OMA; IFCTVGE; -.
DR PhylomeDB; P44468; -.
DR BioCyc; HINF71421:G1GJ1-31-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
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; IBA:GO_Central.
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 PANTHER; PTHR30474; PTHR30474; 1.
DR PANTHER; PTHR30474:SF1; PTHR30474:SF1; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR TIGRFAMs; TIGR02210; rodA_shape; 1.
DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..371
FT /note="Peptidoglycan glycosyltransferase MrdB"
FT /id="PRO_0000062717"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
SQ SEQUENCE 371 AA; 41164 MW; 85D5DDDE60B87E30 CRC64;
MEDKIPFWLR VWQRLHIDFW LFIGLLAITA YGMLVLYSAS GASETMFNSR IIQVLLGFIV
MLLMAQFPPR FYQRIAPYLY LIGFVLLILV DVIGTTSKGA QRWLDLGFIR FQPSEIVKLA
VPLMVAVYLG NRPLPPKLSE TFIAIAMILL PTLLVAIQPD LGTSILVSAS GLFVVFLAGM
SWWLILAAVI GLAGFIPIMW LYLMHDYQRT RVLTLLDPEK DPLGAGYHIL QSKIAIGSGG
LSGKGWMQGT QSQLEFLPEP HTDFIFAVMG EEHGMIGFLI LMAIYLFIIV RGLMIAVNAQ
TSFGRILAGA TTLIFFVYVF VNIGMVSGIL PVVGVPLPLF SYGGTSYVAI MASFGLLMSI
HTHKSQFMKR S
