ID F4SUT1_ECOLX Unreviewed; 397 AA.
AC F4SUT1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acriflavine resistance protein A {ECO:0000313|EMBL:EGI16527.1};
GN ORFNames=ECIG_00030 {ECO:0000313|EMBL:EGI16527.1};
OS Escherichia coli M605.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656417 {ECO:0000313|EMBL:EGI16527.1, ECO:0000313|Proteomes:UP000004710};
RN [1] {ECO:0000313|EMBL:EGI16527.1, ECO:0000313|Proteomes:UP000004710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M605 {ECO:0000313|EMBL:EGI16527.1,
RC ECO:0000313|Proteomes:UP000004710};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli M605.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004519}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004519}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477}.
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DR EMBL; GL883901; EGI16527.1; -; Genomic_DNA.
DR RefSeq; WP_001295833.1; NZ_GL883901.1.
DR AlphaFoldDB; F4SUT1; -.
DR SMR; F4SUT1; -.
DR HOGENOM; CLU_018816_2_1_6; -.
DR Proteomes; UP000004710; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProt.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR032317; HlyD_D23.
DR InterPro; IPR006143; RND_pump_MFP.
DR NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30158; ACRA/E-RELATED COMPONENT OF DRUG EFFLUX TRANSPORTER; 1.
DR PANTHER; PTHR30158:SF3; MULTIDRUG EFFLUX PUMP SUBUNIT ACRA-RELATED; 1.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..397
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003322341"
FT DOMAIN 38..360
FT /note="Cation efflux system protein CusB"
FT /evidence="ECO:0000259|Pfam:PF00529"
FT DOMAIN 63..293
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
FT REGION 377..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 42167 MW; 0F9F6D5BC907A6AC CRC64;
MNKNRGFTPL AVVLMLSGSL ALTGCDDKQA QQGGQQMPAV GVVTVKTEPL QITTELPGRT
SAYRIAEVRP QVSGIILKRN FKEGSDIEAG VSLYQIDPAT YQAAYDSAKG DLAKAQAAAN
IAQLTVNRYQ KLLGTQYISK QEYDQALADA QQANAAVTAA KAAVETARIN LAYTKVTSPI
SGRIGKSNVT EGALVQNGQA TALATVQQLD PIYVDVTQSS NDFLRLKQEL ANGTLKQENG
KAKVSLITSD GIKFPQDGTL EFSDVTVDQT TGSITLRAIF PNPDHTLLPG MFVRARLEEG
LNPNAILVPQ QGVTRTPRGD ATVLVVGADD KVETRPIVAS QAIGDKWLVT EGLKAGDRVV
ISGLQKVRPG VQVKAQEVTA DNNQQAASGA QPEQSKS
//
