ID A0A1Y6BGU6_9PROT Unreviewed; 648 AA.
AC A0A1Y6BGU6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Na(+)/H(+) antiporter NhaA {ECO:0000256|HAMAP-Rule:MF_01844};
DE AltName: Full=Sodium/proton antiporter NhaA {ECO:0000256|HAMAP-Rule:MF_01844};
GN Name=nhaA {ECO:0000256|HAMAP-Rule:MF_01844};
GN ORFNames=SAMN05428998_103120 {ECO:0000313|EMBL:SMF03229.1};
OS Tistlia consotensis USBA 355.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Fodinicurvataceae; Tistlia.
OX NCBI_TaxID=560819 {ECO:0000313|EMBL:SMF03229.1, ECO:0000313|Proteomes:UP000192917};
RN [1] {ECO:0000313|EMBL:SMF03229.1, ECO:0000313|Proteomes:UP000192917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 355 {ECO:0000313|EMBL:SMF03229.1,
RC ECO:0000313|Proteomes:UP000192917};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be required for disulfide bond formation in some
CC proteins. {ECO:0000256|ARBA:ARBA00003565}.
CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC external protons. {ECO:0000256|HAMAP-Rule:MF_01844}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out);
CC Xref=Rhea:RHEA:29251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01844};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Cell membrane {ECO:0000256|HAMAP-
CC Rule:MF_01844}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01844}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter
CC family. {ECO:0000256|HAMAP-Rule:MF_01844}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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DR EMBL; FWZX01000003; SMF03229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6BGU6; -.
DR STRING; 560819.SAMN05428998_103120; -.
DR Proteomes; UP000192917; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006885; P:regulation of pH; IEA:InterPro.
DR CDD; cd02972; DsbA_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.20.1530.10; Na+/H+ antiporter like domain; 1.
DR HAMAP; MF_01844; NhaA; 1.
DR InterPro; IPR023171; Na/H_antiporter_dom_sf.
DR InterPro; IPR004670; NhaA.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR00773; NhaA; 1.
DR PANTHER; PTHR30341:SF0; NA(+)_H(+) ANTIPORTER NHAA; 1.
DR PANTHER; PTHR30341; SODIUM ION/PROTON ANTIPORTER NHAA-RELATED; 1.
DR Pfam; PF06965; Na_H_antiport_1; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|HAMAP-Rule:MF_01844};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01844}; Ion transport {ECO:0000256|HAMAP-Rule:MF_01844};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01844};
KW Reference proteome {ECO:0000313|Proteomes:UP000192917};
KW Sodium {ECO:0000256|HAMAP-Rule:MF_01844};
KW Sodium transport {ECO:0000256|HAMAP-Rule:MF_01844};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01844};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01844}; Transport {ECO:0000256|HAMAP-Rule:MF_01844}.
FT TRANSMEM 198..221
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 253..270
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 282..303
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 315..334
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 341..364
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 370..386
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 398..426
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 529..552
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 564..586
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 598..620
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT DOMAIN 1..189
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 648 AA; 68237 MW; 0BB2452ED16B476C CRC64;
MTKGQIPERL RARLQRPVDP ERDHLRGGTA PAGVTTIVLY GDYLCPYCRR LRIVLARLRE
ALGGRLAYVY RHFPNEAAHP GATFLARAAE AAGRQGRFWE MHDWIYEQEL PLAEPQAQVQ
DAARAFGLDL DRFRQDLESE EAGRRVGSDL SEGRRNGVTG TPTLFLDGER YDGAWDFHSM
LEALQLPMAS RLGRSARAFA NLPASGGLVL LLAAAAALLF ANTALAPFYR AFIGLDVGIG
PPGKLLSLNL AEWFSEGLLA VFFTLIGLEI RREVTSGELS SLRAAILPVV GALGGMLAPA
LIYLSLNADG LPEGWAVPTA TDIAFTIGIL ALLGPRVPAS LRVFVAALAV VDDVLSVLTL
AVFYPQDFEP SWLLPAAAAV GLLFLLNRAR VYAAWPYLLT AALLWVCLHA SGVHAALAGI
ALAAFLPTRP APAVAPLLAQ AATALSTLEH AEKQARGTSA GPVSIAGEPL WEWASRNLSA
ASDRLLSPAD RVERAIAPWS TYVILPLFAF SASGVRLDLD MAAPDAGQVL AGMVLGLVVG
KPVGIALASL AAVKTRLAVA PVGVAPGSFV GAAMLCGVGY TVALLLADQA FPDEGYAAVA
KSGVLAGSVL AAALGTLVLM TRPAAARTNA SDQVVLDGKD PAIAENNR
//