(data stored in ACNUC7421 zone)

SWISSPROT: C6AYD1_RHILS

ID   C6AYD1_RHILS            Unreviewed;       526 AA.
AC   C6AYD1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   OrderedLocusNames=Rleg_0044 {ECO:0000313|EMBL:ACS54355.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54355.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54355.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54355.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Involved in peptidoglycan biosynthesis. Transports
CC       lipid-linked peptidoglycan precursors from the inner to the outer
CC       leaflet of the cytoplasmic membrane. {ECO:0000256|HAMAP-
CC       Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02078}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02078}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02078}.
CC   -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000256|HAMAP-
CC       Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
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DR   EMBL; CP001622; ACS54355.1; -; Genomic_DNA.
DR   RefSeq; WP_003544894.1; NC_012850.1.
DR   EnsemblBacteria; ACS54355; ACS54355; Rleg_0044.
DR   KEGG; rlg:Rleg_0044; -.
DR   HOGENOM; HOG000263813; -.
DR   KO; K03980; -.
DR   OMA; IFFVAFK; -.
DR   OrthoDB; POG091H05U3; -.
DR   BioCyc; RLEG395491:GHX2-44-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd13123; MATE_MurJ_like; 1.
DR   HAMAP; MF_02078; MurJ_MviN; 1.
DR   InterPro; IPR004268; MurJ.
DR   Pfam; PF03023; MVIN; 1.
DR   PIRSF; PIRSF002869; MviN; 1.
DR   PRINTS; PR01806; VIRFACTRMVIN.
DR   TIGRFAMs; TIGR01695; murJ_mviN; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6AYD1.
DR   SWISS-2DPAGE; C6AYD1.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02078};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02078,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02078,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02078,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02078,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02078,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02078};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02078};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_02078,
KW   ECO:0000256|PIRNR:PIRNR002869}.
FT   TRANSMEM     90    115       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    127    146       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    158    181       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    193    221       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    233    253       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    273    292       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    313    331       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    351    369       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    389    407       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    413    432       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    444    465       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    485    509       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
SQ   SEQUENCE   526 AA;  56103 MW;  B222903625E5F3EC CRC64;
     MSLVKKFATV GGATLGSRIF GFARETLMAA ALGTGPMADV FYAAFRFPNL FRRLFAEGAF
     NAAFVPLFAK EIEANGTDGA KRFSEEVFGV LFSVLLLITI VMELAMPLLV RFVIAPGFAD
     DPEKFSITIR MAAVMFPYLM CMSLTAMMSG MLNSLHHFFA AAIAPVFLNV VMIGALFYAL
     YTGADPLATA WYLSWGVLAA GVLQLAVVYV GVLAAGMSIG FRFPKMTPNV KRLLILAVPA
     AVTGGITQIN QLIGQAIASS RDGAIAALQY ADRIYQLPLG VVGVAVGVVL LPELARALKG
     GNLREAGNLQ NRSIEFVLFL TIPAAFALWI LSDEIIRVLY ERGAFHQENT AVVGSILAIY
     GIGLPAFVLI KALQPGFYAR EDTKTPMRFS AIAVATNCAT ALTLFPYMGA PGIAVAEATA
     GWISTVLLFA TLLRRGHLTW EWALAKRTAL LIVAAAVMGA AIVFLKQYWA PSLASGAPLL
     TKIGTLGLLI AIAMLIYFAA AFLVGGANLG MIRRNLNRKP APAKDG
//

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