ID A0A1I4GVC9_9MICO Unreviewed; 631 AA.
AC A0A1I4GVC9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN04515692_1035 {ECO:0000313|EMBL:SFL33297.1};
OS Leifsonia sp. CL147.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1798215 {ECO:0000313|EMBL:SFL33297.1, ECO:0000313|Proteomes:UP000198997};
RN [1] {ECO:0000313|Proteomes:UP000198997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL147 {ECO:0000313|Proteomes:UP000198997};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOTM01000003; SFL33297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4GVC9; -.
DR OrthoDB; 117402at2; -.
DR Proteomes; UP000198997; 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 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.
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:UP000198997};
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 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 118..141
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 230..260
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 313..332
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 344..367
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 387..406
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 418..436
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT DOMAIN 459..612
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13462"
SQ SEQUENCE 631 AA; 68188 MW; E93B95D7DABB55A1 CRC64;
MTIPLTLIQR SPDPENVGQS RDRRPTIAER FRAVGRSRLG ALLLLLATIV AIVWANISFT
GYEQFWETHL TFGVGDLHLD FTLHALVNDA LMALFFFTVG LEVRREFAIG ELTSWSRAVV
PVVAAVFGLA VPAVIYVLFT LGTGLEHAWG VVISTDTAFL VGALALIGPR ATGRLRVFLL
ALAVVDDIGA LTIIALVYTQ HFTPLPLIVA ALGLVGVYFT RYLRGGRGPV YATLAIVVWL
AFLASGVHPT LAGVAIALLI PVYRPNRIDV EHALDLARTF RQSPNTEYAR AAANSLRESI
SINERLQSAW SPYVAYVVLP LFALANAGVR LNGDILLGAL VSPIAWGVLV GLVVGKFVGV
FGSAALLRLL RVGEFGPGLA LDRLAGGAAL CGIGFTISLF IVDLAIPGAA MQNAARVGVL
AATVVGFLVA TLIFRISDAR RPKEEVGTTL LRPVDPDRDH IFGSMDAPFE IVEYGDFQCG
FCLKATGSVV EVQRELGDGL RYVWRHAPLT RFHPNALAAA EASEAASRQG KFFEFERSLF
ADQENQLPSD IVRRARELGL DVERFEADLR SAEVAARVRD DMLDAEAMDI TAVPTFFING
RRHSGPYDAQ SLIRDLQATA DGGRLEPSSP A
//