ID D5ZYB7_STRV1 Unreviewed; 626 AA.
AC D5ZYB7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=SSFG_06355 {ECO:0000313|EMBL:EFE71115.2};
OS Streptomyces viridosporus (strain ATCC 14672 / DSM 40746 / JCM 4963 / KCTC
OS 9882 / NRRL B-12104 / FH 1290) (Streptomyces ghanaensis).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE71115.2, ECO:0000313|Proteomes:UP000003824};
RN [1] {ECO:0000313|Proteomes:UP000003824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14672 / DSM 40746 / JCM 4963 / KCTC 9882 / NRRL B-12104 /
RC FH 1290 {ECO:0000313|Proteomes:UP000003824};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces ghanaensis ATCC 14672.";
RL Submitted (DEC-2008) 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}.
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DR EMBL; DS999641; EFE71115.2; -; Genomic_DNA.
DR AlphaFoldDB; D5ZYB7; -.
DR eggNOG; COG1651; Bacteria.
DR eggNOG; COG3004; Bacteria.
DR Proteomes; UP000003824; 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 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 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 88..105
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 143..164
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 176..197
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 230..258
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 311..329
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 383..404
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 416..438
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT DOMAIN 423..621
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 626 AA; 66053 MW; BF4AF970BAD2A467 CRC64;
MQKANVQEDS QTRSRRRTLV AQLSGPVRSF LATEAGSAGL LLAAVVVALV WANSPWSDAY
TSLWATEASF SIGGADLSMS LGHWVSDGLM ALFFFVIGLE VRYEVSVGVL TDRRRVVIPA
LAGIGGMLVP ALLYLVIAPG GDASNGWGVV IGTDTAFMLG ALAVVGPRFV TQLRVFLLAI
TVIDDIVAVA VIGLVFSESV RPLLVLAALA LCVVLAGLSR LGAWRTAPYV LIALALWLVT
FEAGLHASIA GMLGGLLIPA RAPTRQAVDR AARLFRAFRQ SPRPDVGRTA RMGLQRAVSV
NERLQTVLHP WTSYVVVPVF ALASAGVDLR DGVLAEALSS SVTWAVVVGL VIGKLVGLGG
FALGGARLGL GKLPRGVGEG QVLGGAVLSG IGFTVSLLIA GLAFEDPALR AQATVGILLA
ALLSALLGWV VFHLAAVLRG ETEADLPRFL DRPVDPATDH ITGPPDAPLT LVEYGDYECP
FCAHATGVAQ ELQQRFGDRL RYVFRHLPLP DVHEHSELAA RAAVAADAQG RFWQMHDLLF
AHQDQLEFED ILGYAGQIGL DVERFLEDLD SERTAARVRA DVASAEASGA QGAPTFFIGN
RRHTGPYDAQ TLAARLEASG AGGGLA
//
