ID A0A143WU85_9ENTR Unreviewed; 370 AA.
AC A0A143WU85;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:CUX97310.1};
GN Synonyms=rodA {ECO:0000256|HAMAP-Rule:MF_02079};
GN ORFNames=TPER_HE00394 {ECO:0000313|EMBL:CUX97310.1};
OS Candidatus Hoaglandella endobia.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Hoaglandella.
OX NCBI_TaxID=1778263 {ECO:0000313|EMBL:CUX97310.1, ECO:0000313|Proteomes:UP000095477};
RN [1] {ECO:0000313|Proteomes:UP000095477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Husnik F.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; LN999835; CUX97310.1; -; Genomic_DNA.
DR RefSeq; WP_067567940.1; NZ_LN999835.1.
DR AlphaFoldDB; A0A143WU85; -.
DR STRING; 1778263.TPER_HE00394; -.
DR KEGG; hed:TPER_HE00394; -.
DR PATRIC; fig|1778263.3.peg.391; -.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000095477; 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; 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.
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:UP000095477};
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 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 136..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 160..177
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 305..332
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ SEQUENCE 370 AA; 40823 MW; 142C080242F60B42 CRC64;
MTNNQPQISL WKKLHIDVML MLFIILLLVY SAFVVWSASG QDIGIMERKI AQIVTGLLIM
LVMAQVPPRV YEFWAPYLYL FCVFLLVLVE AFGQISKGAQ RWLDLGLVRF QPSEIAKIAV
PLMVARFVNR ESCPPSLKNT TISLILIFVP TLLVAVQPDL GTAILIAASG LLVLFLAGMS
WKLITVAVLW VVAFIPVLWF FLMHDYQRER VMMLLNPEID PLGAGYHIIQ SKIAIGSGGL
FGKGWLHGTQ SQLEFLPERH TDFIFSVLGE ELGLIGVLLL LGLYLGVITR GLIIAAQVPN
TFGRVIAGGL MFILFVYVFV NIGMVSSILP VVGVPLPLVS YGGSALIVLM AGFGMVMSIH
THRKMLSNSL
//
