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 13-FEB-2019, entry version 97. DE RecName: Full=Lipid II flippase MurJ {ECO:0000305}; DE AltName: Full=Peptidoglycan biosynthesis protein MurJ {ECO:0000305}; GN Name=murJ {ECO:0000255|HAMAP-Rule:MF_02078, GN ECO:0000303|PubMed:18832143}; Synonyms=mviN, yceN; GN OrderedLocusNames=b1069, JW1056; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; 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, PROBABLE 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 PROBABLE FUNCTION AS A TRANSPORTER, SUBCELLULAR LOCATION, TOPOLOGY, RP AND MUTAGENESIS OF ARG-18; ARG-24; ASP-39; ARG-52 AND ARG-270. RX PubMed=23935042; DOI=10.1128/JB.00731-13; RA Butler E.K., Davis R.M., Bari V., Nicholson P.A., Ruiz N.; RT "Structure-function analysis of MurJ reveals a solvent-exposed cavity RT containing residues essential for peptidoglycan biogenesis in RT Escherichia coli."; RL J. Bacteriol. 195:4639-4649(2013). RN [8] RP FUNCTION AS A FLIPPASE, AND PATHWAY. RX PubMed=25013077; DOI=10.1126/science.1254522; RA Sham L.T., Butler E.K., Lebar M.D., Kahne D., Bernhardt T.G., Ruiz N.; RT "Bacterial cell wall. MurJ is the flippase of lipid-linked precursors RT for peptidoglycan biogenesis."; RL Science 345:220-222(2014). 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:0000255|HAMAP- CC Rule:MF_02078, ECO:0000269|PubMed:18708495, CC ECO:0000269|PubMed:18832143, ECO:0000269|PubMed:25013077}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:25013077}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_02078, ECO:0000269|PubMed:15919996, CC ECO:0000269|PubMed:23935042}; Multi-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:15919996, CC ECO:0000269|PubMed:23935042}. CC -!- MISCELLANEOUS: FtsW (AC P0ABG4) is also proposed to act as a lipid CC II flippase. The identity of the lipid II flippase is CC controversial with conflicting in vivo and in vitro results. CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000255|HAMAP- CC Rule:MF_02078, ECO:0000305}. 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; WP_001050683.1; NZ_LN832404.1. DR PDB; 6CC4; X-ray; 3.50 A; A=4-511. DR PDBsum; 6CC4; -. DR ProteinModelPortal; P0AF16; -. DR SMR; P0AF16; -. DR BioGrid; 4260079; 316. DR IntAct; P0AF16; 1. DR STRING; 316385.ECDH10B_1140; -. DR TCDB; 2.A.66.4.3; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily. DR PaxDb; P0AF16; -. DR PRIDE; P0AF16; -. DR EnsemblBacteria; AAC74153; AAC74153; b1069. DR EnsemblBacteria; BAA35877; BAA35877; BAA35877. DR GeneID; 945487; -. DR KEGG; ecj:JW1056; -. DR KEGG; eco:b1069; -. DR PATRIC; fig|1411691.4.peg.1199; -. DR EchoBASE; EB3639; -. DR EcoGene; EG13880; murJ. DR eggNOG; ENOG4105CJR; Bacteria. DR eggNOG; COG0728; LUCA. DR HOGENOM; HOG000263812; -. DR InParanoid; P0AF16; -. DR KO; K03980; -. DR PhylomeDB; P0AF16; -. DR BioCyc; EcoCyc:G6561-MONOMER; -. DR BioCyc; ECOL316407:JW1056-MONOMER; -. DR BioCyc; MetaCyc:G6561-MONOMER; -. DR UniPathway; UPA00219; -. DR PRO; PR:P0AF16; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IDA:EcoCyc. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0034203; P:glycolipid translocation; IMP:CACAO. DR GO; GO:0034204; P:lipid translocation; IDA:EcoCyc. DR GO; GO:0015836; P:lipid-linked peptidoglycan transport; IDA:EcoCyc. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc. 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; MurJ; 1. DR PIRSF; PIRSF002869; MviN; 1. DR PRINTS; PR01806; VIRFACTRMVIN. DR TIGRFAMs; TIGR01695; murJ_mviN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Membrane; KW Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 511 Lipid II flippase MurJ. FT /FTId=PRO_0000182006. FT TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 6 32 Helical. {ECO:0000255}. FT TOPO_DOM 33 40 Periplasmic. {ECO:0000255}. FT TRANSMEM 41 69 Helical. {ECO:0000255}. FT TOPO_DOM 70 82 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 83 109 Helical. {ECO:0000255}. FT TOPO_DOM 110 123 Periplasmic. {ECO:0000255}. FT TRANSMEM 124 154 Helical. {ECO:0000255}. FT TOPO_DOM 155 156 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 157 178 Helical. {ECO:0000255}. FT TOPO_DOM 179 185 Periplasmic. {ECO:0000255}. FT TRANSMEM 186 207 Helical. {ECO:0000255}. FT TOPO_DOM 208 223 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 224 253 Helical. {ECO:0000255}. FT TOPO_DOM 254 263 Periplasmic. {ECO:0000255}. FT TRANSMEM 264 292 Helical. {ECO:0000255}. FT TOPO_DOM 293 302 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 303 337 Helical. {ECO:0000255}. FT TOPO_DOM 338 346 Periplasmic. {ECO:0000255}. FT TRANSMEM 347 374 Helical. {ECO:0000255}. FT TOPO_DOM 375 379 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 380 402 Helical. {ECO:0000255}. FT TOPO_DOM 403 409 Periplasmic. {ECO:0000255}. FT TRANSMEM 410 429 Helical. {ECO:0000255}. FT TOPO_DOM 430 443 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 444 463 Helical. {ECO:0000255}. FT TOPO_DOM 464 477 Periplasmic. {ECO:0000255}. FT TRANSMEM 478 499 Helical. {ECO:0000255}. FT TOPO_DOM 500 511 Cytoplasmic. {ECO:0000255}. FT MUTAGEN 18 18 R->A,C: Lack of activity. FT {ECO:0000269|PubMed:23935042}. FT MUTAGEN 24 24 R->A,C: Lack of activity. FT {ECO:0000269|PubMed:23935042}. FT MUTAGEN 39 39 D->A,C: Lack of activity. FT {ECO:0000269|PubMed:23935042}. FT MUTAGEN 52 52 R->A: Decrease in activity. FT {ECO:0000269|PubMed:23935042}. FT MUTAGEN 52 52 R->C: Lack of activity. FT {ECO:0000269|PubMed:23935042}. FT MUTAGEN 270 270 R->A,C: Lack of activity. FT {ECO:0000269|PubMed:23935042}. FT HELIX 7 11 {ECO:0000244|PDB:6CC4}. FT HELIX 15 32 {ECO:0000244|PDB:6CC4}. FT HELIX 36 55 {ECO:0000244|PDB:6CC4}. FT HELIX 58 73 {ECO:0000244|PDB:6CC4}. FT HELIX 77 104 {ECO:0000244|PDB:6CC4}. FT HELIX 106 113 {ECO:0000244|PDB:6CC4}. FT HELIX 115 119 {ECO:0000244|PDB:6CC4}. FT STRAND 120 122 {ECO:0000244|PDB:6CC4}. FT HELIX 123 134 {ECO:0000244|PDB:6CC4}. FT HELIX 137 154 {ECO:0000244|PDB:6CC4}. FT HELIX 158 178 {ECO:0000244|PDB:6CC4}. FT TURN 179 181 {ECO:0000244|PDB:6CC4}. FT STRAND 182 184 {ECO:0000244|PDB:6CC4}. FT HELIX 186 210 {ECO:0000244|PDB:6CC4}. FT HELIX 224 255 {ECO:0000244|PDB:6CC4}. FT HELIX 261 286 {ECO:0000244|PDB:6CC4}. FT HELIX 288 296 {ECO:0000244|PDB:6CC4}. FT HELIX 300 327 {ECO:0000244|PDB:6CC4}. FT HELIX 329 337 {ECO:0000244|PDB:6CC4}. FT HELIX 344 358 {ECO:0000244|PDB:6CC4}. FT HELIX 360 376 {ECO:0000244|PDB:6CC4}. FT HELIX 383 405 {ECO:0000244|PDB:6CC4}. FT HELIX 407 431 {ECO:0000244|PDB:6CC4}. FT HELIX 441 465 {ECO:0000244|PDB:6CC4}. FT HELIX 474 498 {ECO:0000244|PDB:6CC4}. 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 //