ID   EMRA_ACIBT              Reviewed;         353 AA.
AC   P0DPR6;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Colistin resistance protein EmrA {ECO:0000305};
GN   Name=emrA {ECO:0000303|PubMed:28120193};
GN   OrderedLocusNames=A1S_1773 {ECO:0000312|EMBL:ABO12200.2};
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, AND INDUCTION.
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}; Single-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Cotranscribed with emrB. Induced during osmotic stress.
CC       {ECO:0000269|PubMed:28120193}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABO12200.2; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000521; ABO12200.2; ALT_TERM; Genomic_DNA.
DR   AlphaFoldDB; P0DPR6; -.
DR   SMR; P0DPR6; -.
DR   KEGG; acb:A1S_1773; -.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Coiled coil;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..353
FT                   /note="Colistin resistance protein EmrA"
FT                   /id="PRO_0000445981"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   COILED          132..204
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   353 AA;  38896 MW;  BC6A1AEB69F27BEE CRC64;
     MDNVAQLETD TNFQSRKKIT WGVFSVLLLF LVAGILYYFF VYRFYQSTDN AYVQADVTWV
     MPKISGEVME LLINDNQVVK KGETLAVLDH RDYQARYDQA RSVVSLKEAA LGVQQQNEKS
     ARSSIIEANS GVVAAQADLA RLKKEFERYQ DLLKDGVITR QNFEGIQSQY LTAQAQLSKA
     QAAVNAAEAQ LGSLQASRAQ LLADIQSSHA NLNLYQVDLA SSKVVSPVSG KIGSLAIQKG
     SRVSPQTRLM AIIPENSLYV QANFKETQIE KMHIGQKVKL KLDAYPSLNF TGKIESFSPA
     SGATFSLMPP DNATGNFNKV VQRIPVRIAI DSSPHIDLVK PGMSVSATVD LRT