NQRA_VIBCH
ID NQRA_VIBCH Reviewed; 446 AA.
AC Q9KPS1; Q9X4Q3;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit A {ECO:0000255|HAMAP-Rule:MF_00425};
DE Short=Na(+)-NQR subunit A {ECO:0000255|HAMAP-Rule:MF_00425};
DE Short=Na(+)-translocating NQR subunit A {ECO:0000255|HAMAP-Rule:MF_00425};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00425};
DE AltName: Full=NQR complex subunit A {ECO:0000255|HAMAP-Rule:MF_00425};
DE AltName: Full=NQR-1 subunit A {ECO:0000255|HAMAP-Rule:MF_00425};
GN Name=nqrA {ECO:0000255|HAMAP-Rule:MF_00425}; OrderedLocusNames=VC_2295;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10077658; DOI=10.1073/pnas.96.6.3183;
RA Haese C.C., Mekalanos J.J.;
RT "Effects of changes in membrane sodium flux on virulence gene expression in
RT Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3183-3187(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC ubiquinol by two successive reactions, coupled with the transport of
CC Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are
CC probably involved in the second step, the conversion of ubisemiquinone
CC to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00425}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n
CC Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00425};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00425}.
CC -!- SIMILARITY: Belongs to the NqrA family. {ECO:0000255|HAMAP-
CC Rule:MF_00425}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF95439.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF117331; AAD29962.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95439.1; ALT_INIT; Genomic_DNA.
DR PIR; G82094; G82094.
DR RefSeq; NP_231926.1; NC_002505.1.
DR RefSeq; WP_001906078.1; NZ_LT906614.1.
DR PDB; 4P6V; X-ray; 3.50 A; A=1-446.
DR PDB; 4U9O; X-ray; 1.60 A; A=1-357.
DR PDB; 4U9Q; X-ray; 2.10 A; A/B=1-357.
DR PDBsum; 4P6V; -.
DR PDBsum; 4U9O; -.
DR PDBsum; 4U9Q; -.
DR AlphaFoldDB; Q9KPS1; -.
DR SMR; Q9KPS1; -.
DR DIP; DIP-61337N; -.
DR IntAct; Q9KPS1; 5.
DR STRING; 243277.VC_2295; -.
DR DNASU; 2613091; -.
DR EnsemblBacteria; AAF95439; AAF95439; VC_2295.
DR GeneID; 57740916; -.
DR KEGG; vch:VC_2295; -.
DR PATRIC; fig|243277.26.peg.2189; -.
DR eggNOG; COG1726; Bacteria.
DR HOGENOM; CLU_046656_0_0_6; -.
DR OMA; IKQRPYD; -.
DR BioCyc; MetaCyc:MON-16197; -.
DR BRENDA; 7.2.1.1; 15862.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00425; NqrA; 1.
DR InterPro; IPR008703; NqrA.
DR InterPro; IPR022615; NqrA_C_domain.
DR PANTHER; PTHR37839; PTHR37839; 1.
DR Pfam; PF05896; NQRA; 1.
DR Pfam; PF11973; NQRA_SLBB; 1.
DR TIGRFAMs; TIGR01936; nqrA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion transport; NAD; Reference proteome; Sodium;
KW Sodium transport; Translocase; Transport; Ubiquinone.
FT CHAIN 1..446
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT A"
FT /id="PRO_0000214205"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4U9O"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:4U9Q"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:4U9Q"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:4U9O"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:4U9O"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:4U9O"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 417..423
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 431..444
FT /evidence="ECO:0007829|PDB:4P6V"
SQ SEQUENCE 446 AA; 48624 MW; 428E8C397EBA163D CRC64;
MITIKKGLDL PIAGTPSQVI SDGKAIKKVA LLGEEYVGMR PTMHVRVGDE VKKAQILFED
KKNPGVKFTS PVSGKVVEIN RGAKRVLQSV VIEVAGDDQV TFDKFEANQL ASLNRDAIKT
QLVESGLWTA FRTRPFSKVP AIDSTSEAIF VTAMDTNPLA AEPTVVINEQ SEAFVAGLDV
LSALTTGKVY VCKKGTSLPR SQQPNVEEHV FDGPHPAGLA GTHMHFLYPV SADHVAWSIN
YQDVIAVGQL FLTGELYTQR VVSLAGPVVN KPRLVRTVMG ASLEQLVDSE IMPGEVRIIS
GSVLSGTKAT GPHAYLGRYH LQVSVLREGR DKELFGWAMP GKNKFSVTRS FLGHLFKGQV
YNMTTTTNGS DRSMVPIGNY EKVMPLDMEP TLLLRDLCAG DSDSAVRLGA LELDEEDLAL
CTFVCPGKYE YGQLLRECLD KIEKEG
