MURJ_ECO57
ID MURJ_ECO57 Reviewed; 511 AA.
AC P0AF17; P75932;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000255|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000255|HAMAP-Rule:MF_02078}; Synonyms=mviN;
GN OrderedLocusNames=Z1707, ECs1447;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02078}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02078}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
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DR EMBL; AE005174; AAG55815.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34870.1; -; Genomic_DNA.
DR PIR; G90809; G90809.
DR RefSeq; NP_309474.1; NC_002695.1.
DR RefSeq; WP_001050683.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AF17; -.
DR SMR; P0AF17; -.
DR STRING; 155864.EDL933_1645; -.
DR EnsemblBacteria; AAG55815; AAG55815; Z1707.
DR EnsemblBacteria; BAB34870; BAB34870; ECs_1447.
DR GeneID; 912988; -.
DR KEGG; ece:Z1707; -.
DR KEGG; ecs:ECs_1447; -.
DR PATRIC; fig|386585.9.peg.1548; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_3_6; -.
DR OMA; IFFVAFK; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW 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="Probable lipid II flippase MurJ"
FT /id="PRO_0000182007"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
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