(data stored in ACNUC7421 zone)

SWISSPROT: C3MF00_SINFN

ID   C3MF00_SINFN            Unreviewed;       535 AA.
AC   C3MF00;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-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=mviN {ECO:0000313|EMBL:ACP23837.1};
GN   Synonyms=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   OrderedLocusNames=NGR_c00330 {ECO:0000313|EMBL:ACP23837.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23837.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23837.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001389; ACP23837.1; -; Genomic_DNA.
DR   RefSeq; WP_012706622.1; NC_012587.1.
DR   RefSeq; YP_002824590.1; NC_012587.1.
DR   STRING; 394.NGR_c00330; -.
DR   EnsemblBacteria; ACP23837; ACP23837; NGR_c00330.
DR   GeneID; 7790612; -.
DR   KEGG; rhi:NGR_c00330; -.
DR   PATRIC; fig|394.7.peg.2823; -.
DR   eggNOG; ENOG4105CJR; Bacteria.
DR   eggNOG; COG0728; LUCA.
DR   HOGENOM; HOG000263813; -.
DR   KO; K03980; -.
DR   OMA; IFFVAFK; -.
DR   OrthoDB; POG091H05U3; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001054; 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; C3MF00.
DR   SWISS-2DPAGE; C3MF00.
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:UP000001054};
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   Reference proteome {ECO:0000313|Proteomes:UP000001054};
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     87    110       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    125    146       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    158    181       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    193    212       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    332       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    352    374       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    386    406       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    418    436       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    448    471       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
FT   TRANSMEM    483    509       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02078}.
SQ   SEQUENCE   535 AA;  56690 MW;  879B05DE6BA618A1 CRC64;
     MSLVKKFATV GGATLGSRVF GFVRETFMAA ALGTGPVADA FNTAFRLPNT FRRLFAEGAF
     NAAFVPLFAK EIEARGMEGA RRFSEEVFGV LFTVLLFLTI AMELAMPFIV RELIAPGFAD
     DPAKFASTVT FATIMFPYLA CMSLAAMMAG MLNSLHRYFA AAIAPVFLNV ILIGVLAYAW
     YSGQDPVAVG YGLSWGVMAA GLVQLAIVWI AVRNAGIKIG FRRPRLTANV RRLLVLALPA
     AITGGITQIN LLINTNIASA QEGAVSSLVY ADRIYQLPLG VVGIAVATVL LPELSRALRG
     GNLNEAANLQ NRSVEFTLFL TLPAAAALLV MSEPIVRLLF ERGKFSPEAT VVVGHILAIY
     GLGLPAFVLI KAFIPGFFAR EDTRTPMIFA AISVVVNVSL AVTLFPPLGA SGIATAEIVA
     GWVNALLLFT TLLWRGHWGR DIPLLTRVPR LVIAAAIMAA ALHYAIEWLA FPLSSAAPLA
     VRAATVCGLV AAAMAIYFAS AFGLGGASLG MIRRSLKRRA APAAAPTTGE GPDSP
//

If you have problems or comments...

PBIL Back to PBIL home page