ID   ABAF_ACIBT              Reviewed;         429 AA.
AC   P0DPR5;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Fosfomycin resistance protein AbaF {ECO:0000305};
DE   AltName: Full=Acinetobacter baumannii fosfomycin efflux {ECO:0000303|PubMed:27650185};
GN   Name=abaF {ECO:0000303|PubMed:27650185};
GN   OrderedLocusNames=A1S_1331 {ECO:0000312|EMBL:ABO11759.2};
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=27650185; DOI=10.1093/jac/dkw382;
RA   Sharma A., Sharma R., Bhattacharyya T., Bhando T., Pathania R.;
RT   "Fosfomycin resistance in Acinetobacter baumannii is mediated by efflux
RT   through a major facilitator superfamily (MFS) transporter-AbaF.";
RL   J. Antimicrob. Chemother. 72:68-74(2017).
CC   -!- FUNCTION: Efflux pump that mediates resistance to fosfomycin
CC       (PubMed:27650185). Probably also involved in the secretion of biofilm
CC       matrix that contributes to the pathogenicity (PubMed:27650185).
CC       {ECO:0000269|PubMed:27650185}.
CC   -!- ACTIVITY REGULATION: Inhibited by the efflux inhibitor and energy
CC       decoupler carbonyl cyanide m-chlorophenylhydrazone (CCCP).
CC       {ECO:0000269|PubMed:27650185}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is up-regulated on exposure to fosfomycin.
CC       {ECO:0000269|PubMed:27650185}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene increases susceptibility
CC       to fosfomycin. Disruption also results in impaired biofilm formation
CC       and decreased virulence. {ECO:0000269|PubMed:27650185}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000521; ABO11759.2; -; Genomic_DNA.
DR   RefSeq; WP_000214022.1; NZ_CP053098.1.
DR   AlphaFoldDB; P0DPR5; -.
DR   SMR; P0DPR5; -.
DR   GeneID; 66397637; -.
DR   KEGG; acb:A1S_1331; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..429
FT                   /note="Fosfomycin resistance protein AbaF"
FT                   /id="PRO_0000445973"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   429 AA;  47578 MW;  67F381B26CE07129 CRC64;
     MTTTLKKVVA ASMVGSVAEW YEFFLYGTAS ALVFGELFFQ QTGNAIDGIL AAFALYAVGF
     LARPLGGLVF GHYGDKIGRK KLLQISLIIV GITTFLMGCI PTFHQIGYWA PTLLVILRLI
     QGFAFGGEWG GAVILVSEHS PDDRRGYWAS WPQTGVPLGN LVATLVLLLL SKNLSPEQFL
     DWGWRCAFWF SAVVVLIGLW IRKNVDDAEV FKEAQAKQQL LEKQQLGIIE VLKYHKKSVI
     AGIGARFAEN ILYYMVVTFS ISYLKLVVHK DTSQILLLMF GAHLIHFFII PFMGHLSDIF
     GRKPIYLIGA VLTAFWGFVG FPLMDTGNDW LIMLAIVLGL FIESMTYSPY SALMTELFPT
     HIRYTALSFC YQVAPIMAGS LAPLIALTLL KEFNSSIPIS LYLVAASLIS IVSILLVKET
     KGRSLAFKD