ID   INIA_MYCTU              Reviewed;         640 AA.
AC   P9WJ99; L0T6D8; O06293; Q7D9Z6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Isoniazid-induced protein IniA;
GN   Name=iniA; OrderedLocusNames=Rv0342;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   INDUCTION.
RX   PubMed=10714983; DOI=10.1128/jb.182.7.1802-1811.2000;
RA   Alland D., Steyn A.J., Weisbrod T., Aldrich K., Jacobs W.R. Jr.;
RT   "Characterization of the Mycobacterium tuberculosis iniBAC promoter, a
RT   promoter that responds to cell wall biosynthesis inhibition.";
RL   J. Bacteriol. 182:1802-1811(2000).
RN   [3]
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX   PubMed=15752203; DOI=10.1111/j.1365-2958.2005.04510.x;
RA   Colangeli R., Helb D., Sridharan S., Sun J., Varma-Basil M., Hazbon M.H.,
RA   Harbacheuski R., Megjugorac N.J., Jacobs W.R. Jr., Holzenburg A.,
RA   Sacchettini J.C., Alland D.;
RT   "The Mycobacterium tuberculosis iniA gene is essential for activity of an
RT   efflux pump that confers drug tolerance to both isoniazid and ethambutol.";
RL   Mol. Microbiol. 55:1829-1840(2005).
RN   [4]
RP   INDUCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=17590082; DOI=10.1371/journal.ppat.0030087;
RA   Colangeli R., Helb D., Vilcheze C., Hazbon M.H., Lee C.G., Safi H.,
RA   Sayers B., Sardone I., Jones M.B., Fleischmann R.D., Peterson S.N.,
RA   Jacobs W.R. Jr., Alland D.;
RT   "Transcriptional regulation of multi-drug tolerance and antibiotic-induced
RT   responses by the histone-like protein Lsr2 in M. tuberculosis.";
RL   PLoS Pathog. 3:E87-E87(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Participates in the development of tolerance to both
CC       isoniazid and ethambutol. May function through a MDR-pump like
CC       mechanism, although it does not appear to directly transport isoniazid
CC       from the cell. {ECO:0000269|PubMed:15752203}.
CC   -!- SUBUNIT: Forms multimeric structures containing a central pore.
CC       {ECO:0000269|PubMed:15752203}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Specifically induced by a broad range of inhibitors of cell
CC       wall biosynthesis, including antibiotics that inhibit the synthesis of
CC       peptidoglycan (ampicillin), arabinogalactam (ethambutol), mycolic acids
CC       (isoniazid, ethionamide) and fatty acids (5-chloropyrazinamide). Down-
CC       regulated by the nucleoid-associated protein Lsr2.
CC       {ECO:0000269|PubMed:10714983, ECO:0000269|PubMed:17590082}.
CC   -!- DISRUPTION PHENOTYPE: Deletion results in increased susceptibility to
CC       isoniazid and accumulation of intracellular ethidium bromide.
CC       {ECO:0000269|PubMed:15752203}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL123456; CCP43072.1; -; Genomic_DNA.
DR   PIR; G70573; G70573.
DR   RefSeq; NP_214856.1; NC_000962.3.
DR   RefSeq; WP_003900124.1; NC_000962.3.
DR   AlphaFoldDB; P9WJ99; -.
DR   SMR; P9WJ99; -.
DR   STRING; 83332.Rv0342; -.
DR   TCDB; 9.B.282.1.1; the isoniazid-resistance (iniabc) family.
DR   PaxDb; P9WJ99; -.
DR   PRIDE; P9WJ99; -.
DR   DNASU; 886510; -.
DR   GeneID; 886510; -.
DR   KEGG; mtu:Rv0342; -.
DR   PATRIC; fig|83332.111.peg.378; -.
DR   TubercuList; Rv0342; -.
DR   eggNOG; COG0699; Bacteria.
DR   OMA; CPVDDDI; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:MTBBASE.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell membrane; Coiled coil; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..640
FT                   /note="Isoniazid-induced protein IniA"
FT                   /id="PRO_0000390791"
FT   TRANSMEM        497..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   COILED          560..628
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   640 AA;  70083 MW;  3A28E3E82C528F44 CRC64;
     MVPAGLCAYR DLRRKRARKW GDTVTQPDDP RRVGVIVELI DHTIAIAKLN ERGDLVQRLT
     RARQRITDPQ VRVVIAGLLK QGKSQLLNSL LNLPAARVGD DEATVVITVV SYSAQPSARL
     VLAAGPDGTT AAVDIPVDDI STDVRRAPHA GGREVLRVEV GAPSPLLRGG LAFIDTPGVG
     GLGQPHLSAT LGLLPEADAV LVVSDTSQEF TEPEMWFVRQ AHQICPVGAV VATKTDLYPR
     WREIVNANAA HLQRARVPMP IIAVSSLLRS HAVTLNDKEL NEESNFPAIV KFLSEQVLSR
     ATERVRAGVL GEIRSATEQL AVSLGSELSV VNDPNLRDRL ASDLERRKRE AQQAVQQTAL
     WQQVLGDGFN DLTADVDHDL RTRFRTVTED AERQIDSCDP TAHWAEIGND VENAIATAVG
     DNFVWAYQRS EALADDVARS FADAGLDSVL SAELSPHVMG TDFGRLKALG RMESKPLRRG
     HKMIIGMRGS YGGVVMIGML SSVVGLGLFN PLSVGAGLIL GRMAYKEDKQ NRLLRVRSEA
     KANVRRFVDD ISFVVSKQSR DRLKMIQRLL RDHYREIAEE ITRSLTESLQ ATIAAAQVAE
     TERDNRIREL QRQLGILSQV NDNLAGLEPT LTPRASLGRA