RODA_TREPA
ID RODA_TREPA Reviewed; 433 AA.
AC O83514;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Peptidoglycan glycosyltransferase RodA {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=rodA {ECO:0000255|HAMAP-Rule:MF_02079}; Synonyms=mrdB;
GN OrderedLocusNames=TP_0501;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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}.
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DR EMBL; AE000520; AAC65488.1; -; Genomic_DNA.
DR PIR; A71317; A71317.
DR RefSeq; WP_010881950.1; NC_021490.2.
DR AlphaFoldDB; O83514; -.
DR SMR; O83514; -.
DR IntAct; O83514; 11.
DR STRING; 243276.TPANIC_0501; -.
DR EnsemblBacteria; AAC65488; AAC65488; TP_0501.
DR GeneID; 57879022; -.
DR KEGG; tpa:TP_0501; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_2_2_12; -.
DR OMA; IFCTVGE; -.
DR OrthoDB; 1133883at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR30474; PTHR30474; 1.
DR PANTHER; PTHR30474:SF1; PTHR30474:SF1; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 2.
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..433
FT /note="Peptidoglycan glycosyltransferase RodA"
FT /id="PRO_0000062721"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
SQ SEQUENCE 433 AA; 48345 MW; 19C2EAE3187A3669 CRC64;
MRIRGVSDFD YLLLLTMLAL TSIGILFIYS SGVNSEGHVI SREYLKQIVW AVMGVVLMLS
VSMYDYHRFK DRTTLIFAGF ILLLIYTRLF GRYVNGAKSW IGVGEFGIQI SEFAKIAYIL
YLAHYLVYSQ SEPMLKRFAK AGVITLLPMA LILSQPDLGT ASVYLPIFLV MCFIAGFPLR
LIFAVVCVVL LTLLFTLLPL WEQTFLQYQG VATRIADSRM LSLFVFFSLS ATSAVAVVGY
LLSGRKYYYW ITYALGMVSI SYGASLLGVR VLKPYQMMRL IIFLNPEVDP LKAGWHIIQS
MIAIGSGGAF GMGYLRGPQS HYRFLPQQST DFIFSILSEE WGFVGGVIVF GLYLLFFLHT
LSIMSHVDDL YGKLIASGVL GMFLFHFVVN VGMTMGIMPI TGIPLLLLSY GGSSLWTAMI
ATGLLMSINA RQL
