ID A0A2B8ARI3_9ACTN Unreviewed; 599 AA.
AC A0A2B8ARI3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ECO:0000313|EMBL:PGH47979.1};
GN ORFNames=CRI70_25580 {ECO:0000313|EMBL:PGH47979.1};
OS Streptomyces sp. Ru87.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2044307 {ECO:0000313|EMBL:PGH47979.1, ECO:0000313|Proteomes:UP000222409};
RN [1] {ECO:0000313|EMBL:PGH47979.1, ECO:0000313|Proteomes:UP000222409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru87 {ECO:0000313|EMBL:PGH47979.1,
RC ECO:0000313|Proteomes:UP000222409};
RA Amin D.H., Borsetto C., Abolmaaty A., Tolba S., Abdallah N.A.,
RA Wellington E.M.H.;
RT "Draft genome sequence of Streptomyces sp. Ru87 isolated from Egyptian
RT soil.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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: In the N-terminal section; belongs to the NhaA Na(+)/H(+)
CC (TC 2.A.33) antiporter family. {ECO:0000256|ARBA:ARBA00007006}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01844}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH47979.1}.
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DR EMBL; PDIX01000417; PGH47979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B8ARI3; -.
DR OrthoDB; 117402at2; -.
DR Proteomes; UP000222409; 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 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|ARBA:ARBA00022449, ECO:0000256|HAMAP-Rule:MF_01844};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01844};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01844};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01844};
KW Reference proteome {ECO:0000313|Proteomes:UP000222409};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_01844};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201, ECO:0000256|HAMAP-
KW 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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01844}.
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 149..170
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 176..192
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 321..344
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 390..412
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT DOMAIN 397..595
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 599 AA; 62994 MW; 905884B2C14792AE CRC64;
MRAFTRTEAG SAGMLLAASA VALAWANSPW SASYEALWET HASVRAGAAE LDLDLRHWVN
DGLMGLFFFV IGLEVRREFS LGELTDRRRA VLPVVAALGG MAVPAVLYLA LNPSGAAAGG
WGVVIGTDTA FLLGTLALVG PEFSTQLRLF LLTLTVIDDI VAVSVIGVVY SDSLRVPPLL
AAGCCLLVLA VLSRRGAWRA SVYVVVVCAL WLATEESGLH ASIAGMAAGL LVAARAPRRQ
EVEGAASLFR AFRQSPMPGV GASAKAGLAR AISVNERLQT ALHPWTGFVV VPLFALANAG
IDLRGGVLTD ALTSPVTWGV VLGLSAGKPA GIAAGALGGA RLGLGRLPQG VGPGQVLGGA
ALSGIGFTVS LLIVQLAFED RALRDEATVG VLLAAVVSTL TGWVAFRLAA VLRGERTADL
PRVLDRPVRT GTDHVRGPAD APLTLVEYGD FECPFCAKAT GVARELRERF GDDLRYVFRH
LPLPDVHPRA EAAARAAESA AAQDRFWEMH DLLFRHQDEL EYEDLAGYAA ELGLDVERFL
RDLDDERTAA RIRADVAGAE ASGARGTPTF FVGDRRHTGP HDTESLAAAL GSLRTTASG
//
