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Database: UniProt
Entry: A0A0K8P1K9_IDESA
LinkDB: A0A0K8P1K9_IDESA
Original site: A0A0K8P1K9_IDESA 
ID   A0A0K8P1K9_IDESA        Unreviewed;       385 AA.
AC   A0A0K8P1K9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   Synonyms=rodA {ECO:0000256|HAMAP-Rule:MF_02079};
GN   ORFNames=ISF6_2264 {ECO:0000313|EMBL:GAP36424.1};
OS   Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Ideonella.
OX   NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP36424.1, ECO:0000313|Proteomes:UP000037660};
RN   [1] {ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC   {ECO:0000313|Proteomes:UP000037660};
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "Discovery of a poly(ethylene terephthalate assimilation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAP36424.1, ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC   {ECO:0000313|Proteomes:UP000037660};
RX   PubMed=26965627; DOI=10.1126/science.aad6359;
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL   Science 351:1196-1199(2016).
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}.
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:GAP36424.1}.
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DR   EMBL; BBYR01000035; GAP36424.1; -; Genomic_DNA.
DR   RefSeq; WP_054020420.1; NZ_BBYR01000035.1.
DR   AlphaFoldDB; A0A0K8P1K9; -.
DR   STRING; 1547922.ISF6_2264; -.
DR   OMA; IFCTVGE; -.
DR   OrthoDB; 9768187at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000037660; 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; 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:UP000037660};
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        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        57..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        142..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        165..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        189..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        289..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        322..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        355..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ   SEQUENCE   385 AA;  41365 MW;  900665014EF8BFF7 CRC64;
     MNVAFNKPSL LQRLAPVFSG FDGPLLLALL MLGSAGLVTM YSVGFDHGTR FVDHGRNMVL
     AAGILFVVAQ VPPQRLMNLA VPLYVLGVTL LVATALFGLT KKGATRWLDL QVTVIQPSEI
     LKIATPLMLA WWFQRREGQL RIPDFLVAVL LLAIPVGLIA KQPDLGTALL VLSTGLYVMF
     FAGLSWRLIL PVLAVAAVGI GTLVFTGDDI CQPGVEWPVL HEYQRHRVCT LLDPSKDPLG
     KGFHIIQGMI AIGSGGLDGK GFMKGTQTHL EFIPERTTDF VFAAFAEEFG LIGCGLLLAG
     FLFLIFRGLM IAADAPTVFT RLLAGALTMS FFTYAFVNMG MVSGILPVVG VPLPFISYGG
     TAMVTLGCGL GVLMSIAKSR RLVQS
//
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