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 25-MAY-2022, entry version 113. 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, ECO:0000303|PubMed:18832143}; GN Synonyms=mviN, yceN; 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., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT 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., Mau B., RA 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 MG1655 RT 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 Escherichia RT 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 lipid II RT 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, AND RP 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 Escherichia RT 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 for RT peptidoglycan biogenesis."; RL Science 345:220-222(2014). CC -!- FUNCTION: Involved in peptidoglycan biosynthesis. Transports lipid- CC linked peptidoglycan precursors from the inner to the outer leaflet of CC the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_02078, CC ECO:0000269|PubMed:18708495, ECO:0000269|PubMed:18832143, CC 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 II CC flippase. The identity of the lipid II flippase is controversial with CC 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_SSZK01000053.1. DR PDB; 6CC4; X-ray; 3.50 A; A=4-511. DR PDBsum; 6CC4; -. DR AlphaFoldDB; P0AF16; -. DR SMR; P0AF16; -. DR BioGRID; 4260079; 316. DR IntAct; P0AF16; 1. DR STRING; 511145.b1069; -. 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 eggNOG; COG0728; Bacteria. DR HOGENOM; CLU_006797_5_3_6; -. DR InParanoid; P0AF16; -. DR OMA; IFFVAFK; -. DR PhylomeDB; P0AF16; -. DR BioCyc; EcoCyc:G6561-MONOMER; -. DR UniPathway; UPA00219; -. DR PRO; PR:P0AF16; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0000935; C:division septum; IDA:EcoCyc. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:1901612; F:cardiolipin binding; 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; IBA:GO_Central. 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; Membrane; Peptidoglycan synthesis; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..511 FT /note="Lipid II flippase MurJ" FT /id="PRO_0000182006" FT TOPO_DOM 1..5 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 6..32 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 33..40 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 41..69 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 70..82 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 83..109 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 110..123 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 124..154 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 155..156 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 157..178 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 179..185 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 186..207 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 208..223 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 224..253 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 254..263 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 264..292 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 293..302 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 303..337 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 338..346 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 347..374 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 375..379 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 380..402 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 403..409 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 410..429 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 430..443 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 444..463 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 464..477 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 478..499 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 500..511 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MUTAGEN 18 FT /note="R->A,C: Lack of activity." FT /evidence="ECO:0000269|PubMed:23935042" FT MUTAGEN 24 FT /note="R->A,C: Lack of activity." FT /evidence="ECO:0000269|PubMed:23935042" FT MUTAGEN 39 FT /note="D->A,C: Lack of activity." FT /evidence="ECO:0000269|PubMed:23935042" FT MUTAGEN 52 FT /note="R->A: Decrease in activity." FT /evidence="ECO:0000269|PubMed:23935042" FT MUTAGEN 52 FT /note="R->C: Lack of activity." FT /evidence="ECO:0000269|PubMed:23935042" FT MUTAGEN 270 FT /note="R->A,C: Lack of activity." FT /evidence="ECO:0000269|PubMed:23935042" FT HELIX 7..11 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 15..32 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 36..55 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 58..73 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 77..104 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 106..113 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 115..119 FT /evidence="ECO:0007829|PDB:6CC4" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 123..134 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 137..154 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 158..178 FT /evidence="ECO:0007829|PDB:6CC4" FT TURN 179..181 FT /evidence="ECO:0007829|PDB:6CC4" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 186..210 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 224..255 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 261..286 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 288..296 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 300..327 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 329..337 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 344..358 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 360..376 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 383..405 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 407..431 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 441..465 FT /evidence="ECO:0007829|PDB:6CC4" FT HELIX 474..498 FT /evidence="ECO:0007829|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 //