ID   EMRB_ACIBT              Reviewed;         512 AA.
AC   P0DPR7;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Colistin resistance protein EmrB {ECO:0000305};
GN   Name=emrB {ECO:0000303|PubMed:28120193};
GN   OrderedLocusNames=A1S_1772 {ECO:0000312|EMBL:ABO12199.2};
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=28120193; DOI=10.1007/s12275-017-6408-5;
RA   Lin M.F., Lin Y.Y., Lan C.Y.;
RT   "Contribution of EmrAB efflux pumps to colistin resistance in Acinetobacter
RT   baumannii.";
RL   J. Microbiol. 55:130-136(2017).
CC   -!- FUNCTION: Probably part of an efflux pump system that contributes to
CC       adaptation to osmotic stress and resistance to colistin.
CC       {ECO:0000269|PubMed:28120193}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Cotranscribed with emrA. Induced during osmotic stress.
CC       {ECO:0000269|PubMed:28120193}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene significantly slows cell
CC       growth in 20% sucrose. The mutant is more susceptible to colistin,
CC       nafcillin, paromomycin, spiramycin and D,L-serine hydroxamate than the
CC       wild type. {ECO:0000269|PubMed:28120193}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB family.
CC       {ECO:0000305}.
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DR   EMBL; CP000521; ABO12199.2; -; Genomic_DNA.
DR   AlphaFoldDB; P0DPR7; -.
DR   SMR; P0DPR7; -.
DR   KEGG; acb:A1S_1772; -.
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; IPR004638; EmrB-like.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00711; efflux_EmrB; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..512
FT                   /note="Colistin resistance protein EmrB"
FT                   /id="PRO_0000445982"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   512 AA;  57149 MW;  AAB8C35115D5422A CRC64;
     MNKHVEAEWR FPAKTAWAIF AAMIFGNFMA ILDIQIVASS LNEVQAGMSA SRYEVTWVQT
     VYLIAEIIAI PMSSIVSRVL STRVYYTMCA IGFTVSSLLC ALSWNLESLL VFRGIQGFMG
     GGMIPTSMTA LYLLFPEPKR SLPLVMFGMI STLGPAIGPT IGGWLTNNFS WHWMFLINII
     PGIIIATVIY SGPNIDRANY SLIKSMDWFS LVGMAMFLGG LEYFLDEGAR HDWLADTGVR
     IAFMVCVVGG MIFFSRSFTQ PKPLLDLSVF KNKNFTLSAI TTFVIGMALY GLGYMIPVFL
     GQVREMNSSQ IGHVMMVTGI VMFCFAPFLA WLIPNFDTRK TVFVGMILAG FGVWLNSHLS
     IHSDYDFMFW PQIYRGIGLM ICLIVVSHLA MSTLPLSKVA DASGIYNLMR NIGGAVGLAL
     INSSLDWLTA MHVTQINQSM TPQNWIFTER LDQLTAQYQE VGTNAQQIAL SVIYRDIHFQ
     ALTSSFNDLL RMLAIIMFVT AFLTIFMDRG KK