GenomeNet

Database: UniProt
Entry: A0A3S1AT44_ANAVA
LinkDB: A0A3S1AT44_ANAVA
Original site: A0A3S1AT44_ANAVA 
ID   A0A3S1AT44_ANAVA        Unreviewed;       444 AA.
AC   A0A3S1AT44;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Peptidoglycan glycosyltransferase RodA {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=rodA {ECO:0000256|HAMAP-Rule:MF_02079};
GN   ORFNames=DSM107003_07770 {ECO:0000313|EMBL:RUS98758.1};
OS   Trichormus variabilis SAG 1403-4b.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=447716 {ECO:0000313|EMBL:RUS98758.1, ECO:0000313|Proteomes:UP000276103};
RN   [1] {ECO:0000313|EMBL:RUS98758.1, ECO:0000313|Proteomes:UP000276103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 1403-4b {ECO:0000313|EMBL:RUS98758.1,
RC   ECO:0000313|Proteomes:UP000276103};
RX   PubMed=30590650;
RA   Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA   Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA   Neumann-Schaal M., Petersen J.;
RT   "Day and night: Metabolic profiles and evolutionary relationships of six
RT   axenic non-marine cyanobacteria.";
RL   Genome Biol. Evol. 0:0-0(2018).
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 membrane {ECO:0000256|HAMAP-Rule:MF_02079};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02079}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SEDS family. MrdB/RodA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02079}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUS98758.1}.
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; RSCM01000002; RUS98758.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S1AT44; -.
DR   OrthoDB; 9768187at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000276103; Unassembled WGS sequence.
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; NF037961; RodA_shape; 1.
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; 2.
PE   3: Inferred from homology;
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:UP000276103};
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        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        54..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        109..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        142..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        166..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        190..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        221..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        252..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        379..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        416..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ   SEQUENCE   444 AA;  49325 MW;  4FFC747652276D55 CRC64;
     MLLKPSLPKI RWQYWVKPWQ QVDWLLFCLP VALSMFGGLM ILSTELKQPV TDWWWHWLVA
     GIGSIIALFL ARCRYENLIQ WHWITYALTN FSLMIVLVAG TSAKGAQRWI SIGGFNVQPS
     EFAKIGIIIT LAALLHRRTA STLDSVFRVL AITAIPWALI FLQPDLATSL VFGAIVLGML
     YWANANPGWL ILMISPVVSA ILFSISWPLS SPIVLLKELS FSPLGLAWAG AMGIVGWQTL
     PWRRFNLGAL PLASGAIAAF TLNMLGGELG VFAWNHVLKE YQKDRLSVFI NPEHDPLGAG
     YHLIQSRIAI GAGEVWGWGL FKGPMTQLNF VPEQHTDFIF SAVGEEFGFV GCLIVLFVFC
     LICFRLLHVA QTAKDNFGSL LAIGVLSMIV FQLIVNVGMT VGLAPVAGIP LPWMSYGRSA
     MLTNFIALGI VESVANFRQR QKYY
//
DBGET integrated database retrieval system