ID MURJ_ECOLI Reviewed; 511 AA. AC P0AF16; P75932; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 16-APR-2014, entry version 71. DE RecName: Full=Probable peptidoglycan biosynthesis protein MurJ; GN Name=murJ; Synonyms=mviN, yceN; OrderedLocusNames=b1069, JW1056; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP SUBCELLULAR LOCATION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15919996; DOI=10.1126/science.1109730; RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; RT "Global topology analysis of the Escherichia coli inner membrane RT proteome."; RL Science 308:1321-1323(2005). RN [5] RP FUNCTION IN PEPTIDOGLYCAN BIOSYNTHESIS. RX PubMed=18708495; DOI=10.1128/JB.00551-08; RA Inoue A., Murata Y., Takahashi H., Tsuji N., Fujisaki S., Kato J.; RT "Involvement of an essential gene, mviN, in murein synthesis in RT Escherichia coli."; RL J. Bacteriol. 190:7298-7301(2008). RN [6] RP FUNCTION IN PEPTIDOGLYCAN BIOSYNTHESIS, PROPOSED FUNCTION IN LIPID II RP TRANSLOCATION, AND GENE NAME. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=18832143; DOI=10.1073/pnas.0808352105; RA Ruiz N.; RT "Bioinformatics identification of MurJ (MviN) as the peptidoglycan RT lipid II flippase in Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15553-15557(2008). RN [7] RP SHOWS THAT IT HAS NO DIRECT ROLE IN LIPID II TRANSLOCATION. RX PubMed=21386816; DOI=10.1038/emboj.2011.61; RA Mohammadi T., van Dam V., Sijbrandi R., Vernet T., Zapun A., RA Bouhss A., Diepeveen-de Bruin M., Nguyen-Disteche M., de Kruijff B., RA Breukink E.; RT "Identification of FtsW as a transporter of lipid-linked cell wall RT precursors across the membrane."; RL EMBO J. 30:1425-1432(2011). CC -!- FUNCTION: Involved in peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the MurJ/MviN family. CC -!- CAUTION: Was originally (PubMed:18832143) thought to be a lipid II CC flippase. It was shown later that it has no direct role in lipid CC II translocation (PubMed:21386816). 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; U00096; AAC74153.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35877.1; -; Genomic_DNA. DR PIR; B64850; B64850. DR RefSeq; NP_415587.1; NC_000913.3. DR RefSeq; YP_489337.1; NC_007779.1. DR ProteinModelPortal; P0AF16; -. DR IntAct; P0AF16; 1. DR STRING; 511145.b1069; -. DR TCDB; 2.A.66.4.3; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily. DR EnsemblBacteria; AAC74153; AAC74153; b1069. DR EnsemblBacteria; BAA35877; BAA35877; BAA35877. DR GeneID; 12931085; -. DR GeneID; 945487; -. DR KEGG; ecj:Y75_p1039; -. DR KEGG; eco:b1069; -. DR PATRIC; 32117377; VBIEscCol129921_1111. DR EchoBASE; EB3639; -. DR EcoGene; EG13880; murJ. DR eggNOG; COG0728; -. DR HOGENOM; HOG000263812; -. DR KO; K03980; -. DR OMA; EDTKTPM; -. DR OrthoDB; EOG6C0131; -. DR PhylomeDB; P0AF16; -. DR ProtClustDB; CLSK868744; -. DR BioCyc; EcoCyc:G6561-MONOMER; -. DR BioCyc; ECOL316407:JW1056-MONOMER; -. DR PRO; PR:P0AF16; -. DR Genevestigator; P0AF16; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005319; F:lipid transporter activity; IMP:EcoCyc. DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IMP:EcoCyc. DR GO; GO:0034204; P:lipid translocation; IMP:EcoCyc. DR GO; GO:0015836; P:lipid-linked peptidoglycan transport; IMP:EcoCyc. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc. DR InterPro; IPR004268; Flagellin_assembly_MviN. DR Pfam; PF03023; MVIN; 1. DR PIRSF; PIRSF002869; MviN; 1. DR PRINTS; PR01806; VIRFACTRMVIN. DR TIGRFAMs; TIGR01695; mviN; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 511 Probable peptidoglycan biosynthesis FT protein MurJ. FT /FTId=PRO_0000182006. FT TRANSMEM 31 51 Helical; (Potential). FT TRANSMEM 90 110 Helical; (Potential). FT TRANSMEM 130 150 Helical; (Potential). FT TRANSMEM 159 179 Helical; (Potential). FT TRANSMEM 182 202 Helical; (Potential). FT TRANSMEM 237 257 Helical; (Potential). FT TRANSMEM 271 291 Helical; (Potential). FT TRANSMEM 314 334 Helical; (Potential). FT TRANSMEM 354 374 Helical; (Potential). FT TRANSMEM 383 403 Helical; (Potential). FT TRANSMEM 407 427 Helical; (Potential). FT TRANSMEM 443 463 Helical; (Potential). FT TRANSMEM 481 501 Helical; (Potential). SQ SEQUENCE 511 AA; 55267 MW; CB20FE3CFC9419C2 CRC64; MNLLKSLAAV SSMTMFSRVL GFARDAIVAR IFGAGMATDA FFVAFKLPNL LRRIFAEGAF SQAFVPILAE YKSKQGEDAT RVFVSYVSGL LTLALAVVTV AGMLAAPWVI MVTAPGFADT ADKFALTSQL LKITFPYILL ISLASLVGAI LNTWNRFSIP AFAPTLLNIS MIGFALFAAP YFNPPVLALA WAVTVGGVLQ LVYQLPHLKK IGMLVLPRIN FHDAGAMRVV KQMGPAILGV SVSQISLIIN TIFASFLASG SVSWMYYADR LMEFPSGVLG VALGTILLPS LSKSFASGNH DEYNRLMDWG LRLCFLLALP SAVALGILSG PLTVSLFQYG KFTAFDALMT QRALIAYSVG LIGLIVVKVL APGFYSRQDI KTPVKIAIVT LILTQLMNLA FIGPLKHAGL SLSIGLAACL NASLLYWQLR KQKIFTPQPG WMAFLLRLVV AVLVMSGVLL GMLHIMPEWS LGTMPWRLLR LMAVVLAGIA AYFAALAVLG FKVKEFARRT V //