NHAC_BACSU
ID NHAC_BACSU Reviewed; 453 AA.
AC O07553;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Na(+)/H(+) antiporter NhaC;
DE AltName: Full=Sodium/hydrogen antiporter;
DE AltName: Full=Sodium/proton antiporter;
GN Name=nhaC; Synonyms=yheL; OrderedLocusNames=BSU09680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INVOLVEMENT IN SODIUM UPTAKE.
RX PubMed=10735849; DOI=10.1128/jb.182.8.2088-2095.2000;
RA Wang W., Guffanti A.A., Wei Y., Ito M., Krulwich T.A.;
RT "Two types of Bacillus subtilis tetA(L) deletion strains reveal the
RT physiological importance of TetA(L) in K(+) acquisition as well as in
RT Na(+), alkali, and tetracycline resistance.";
RL J. Bacteriol. 182:2088-2095(2000).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10903309; DOI=10.1074/jbc.m001112200;
RA Wei Y., Guffanti A.A., Ito M., Krulwich T.A.;
RT "Bacillus subtilis YqkI is a novel malic/Na+-lactate antiporter that
RT enhances growth on malate at low protonmotive force.";
RL J. Biol. Chem. 275:30287-30292(2000).
RN [5]
RP CHARACTERIZATION.
RX PubMed=11274110; DOI=10.1128/jb.183.8.2505-2515.2001;
RA Pragai Z., Eschevins C., Bron S., Harwood C.R.;
RT "Bacillus subtilis NhaC, an Na+/H+ antiporter, influences expression of the
RT phoPR operon and production of alkaline phosphatases.";
RL J. Bacteriol. 183:2505-2515(2001).
CC -!- FUNCTION: Is a secondary, electrogenic Na(+)/H(+) antiporter that
CC catalyzes Na(+) uptake and proton efflux. Makes modest contributions to
CC pH homeostasis in the alkaline range of pH but is not contributor to
CC Na(+) resistance. Appears to have a repressive effect on growth and on
CC alkaline phosphatases production in the presence of sodium, by
CC affecting the transcription of the phoP/phoR two-component regulatory
CC system.
CC -!- ACTIVITY REGULATION: The antiport activity is markedly inhibited by
CC both valinomycin and CCCP, and modestly by nigericin.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the NhaC Na(+)/H(+) (TC 2.A.35) antiporter
CC family. {ECO:0000305}.
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DR EMBL; Y14080; CAA74461.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12807.1; -; Genomic_DNA.
DR PIR; D69829; D69829.
DR RefSeq; NP_388849.1; NC_000964.3.
DR RefSeq; WP_003233301.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07553; -.
DR SMR; O07553; -.
DR STRING; 224308.BSU09680; -.
DR TCDB; 2.A.35.1.6; the nhac na(+):h(+) antiporter (nhac) family.
DR PaxDb; O07553; -.
DR PRIDE; O07553; -.
DR EnsemblBacteria; CAB12807; CAB12807; BSU_09680.
DR GeneID; 936274; -.
DR KEGG; bsu:BSU09680; -.
DR PATRIC; fig|224308.179.peg.1041; -.
DR eggNOG; COG1757; Bacteria.
DR InParanoid; O07553; -.
DR OMA; NTCGAYQ; -.
DR PhylomeDB; O07553; -.
DR BioCyc; BSUB:BSU09680-MON; -.
DR Proteomes; UP000001570; 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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR004770; Na/H_antiport_NhaC.
DR InterPro; IPR018461; Na/H_Antiport_NhaC-like_C.
DR Pfam; PF03553; Na_H_antiporter; 1.
DR TIGRFAMs; TIGR00931; antiport_nhaC; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Ion transport; Membrane; Reference proteome;
KW Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..453
FT /note="Na(+)/H(+) antiporter NhaC"
FT /id="PRO_0000052416"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..451
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 453 AA; 48053 MW; 1E1D8103F59235C8 CRC64;
MDSQKKLTFP LAVGLFIFML CIIISCLFLL HVEPHIPLFL SVVMLSAAAL WFGFPWKSIE
KGIVDGIKNG VQPIIVLALI GILIGAWMYS GAIPTMTVYA LSFIEPSHLL LTALFSCMII
STLVGSSLTT VSTIGVALIG VASAAGVPLE WTAGAVICGA CFGDKMSPMS DTTNFAAGIG
EIPIFEHIRH MMGTTIPALL ITVVLFYFLG SSVSADAAST DNIQQVITGI KDAANVTPWA
LLSPLLVVLL AMKRVSVIPV LTAGIISSGI LTAIFVPYSS LQAFMTALQN GTTFETDNEA
AAKIINRGGL QSMMGSVSLI MIAFALGGLM EKIGLISALL EGVMKGIRSK GRLVAATVCS
SIGVNLATGE QYLSILIPGQ SFKSLYDKRN IQRKFLTRSL EDGGTLINPL IPWGVSGAFM
ASALGVPVID YIPFTFFLYI SPMISILIGF VKK
