MURJ_ECOLI
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 03-AUG-2022, entry version 114.
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}.
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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-MON; -.
DR BioCyc; MetaCyc:G6561-MON; -.
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
