INIA_MYCTO
ID INIA_MYCTO Reviewed; 640 AA.
AC P9WJ98; L0T6D8; O06293; Q7D9Z6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Isoniazid-induced protein IniA;
GN Name=iniA; OrderedLocusNames=MT0357;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms multimeric structures containing a central pore.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AE000516; AAK44579.1; -; Genomic_DNA.
DR PIR; G70573; G70573.
DR RefSeq; WP_003900124.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJ98; -.
DR SMR; P9WJ98; -.
DR EnsemblBacteria; AAK44579; AAK44579; MT0357.
DR KEGG; mtc:MT0357; -.
DR PATRIC; fig|83331.31.peg.377; -.
DR HOGENOM; CLU_019977_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
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 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 3: Inferred from homology;
KW Antibiotic resistance; Cell membrane; Coiled coil; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..640
FT /note="Isoniazid-induced protein IniA"
FT /id="PRO_0000427867"
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