ID A0A387B350_9MICO Unreviewed; 626 AA.
AC A0A387B350;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:AYF98024.1};
GN ORFNames=D7I47_06990 {ECO:0000313|EMBL:AYF98024.1};
OS Protaetiibacter intestinalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Protaetiibacter.
OX NCBI_TaxID=2419774 {ECO:0000313|EMBL:AYF98024.1, ECO:0000313|Proteomes:UP000278886};
RN [1] {ECO:0000313|Proteomes:UP000278886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2DFWR-13 {ECO:0000313|Proteomes:UP000278886};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 2DFWR-13.";
RL Submitted (SEP-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP032630; AYF98024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387B350; -.
DR KEGG; lyd:D7I47_06990; -.
DR OrthoDB; 117402at2; -.
DR Proteomes; UP000278886; Chromosome.
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:UP000278886};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 213..240
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 321..345
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 360..383
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01844"
FT DOMAIN 436..593
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13462"
FT REGION 607..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 67067 MW; EE3ED349E5E279D6 CRC64;
MTELITRIRR SPVALRGAVV LIAATLVALT WANLPGEGYA SFWHLPLGFE VGGYTFRLDL
RHWINDAVMA LFFAHVTLEV RRELELGELR DWRRASVPVV AAVAGLVIPA LVFLAVTWGT
EAVHGWGVVV STDTAFVLGM LALVGRGMPP QLRVFLVTLA VADDVGALAV IAFAYTDHFD
PFPLLLAAAG LAAIGVMRLC GVWRGTLYLI PSIVVWVGFL LSGVHATLAG VAIALLLPIF
SARSADVRHA QDHVRAFQLA PSAGSARTAE ESLARTISVN ERAHRALTPY VTWLILPLFA
LANAGVRITP ETLAEAAGSR LTWGIVLGLV VGKIVAISLA SWIMLRARPD ALGDAVRMPH
VFAVSVLAGM GFTISLFVTE LAFADPGQVS SAQIGVLAAT LLAAVLGAVV FGILGRRERS
HAPDRARLSP AFDAHRDRVI GDADAALVTV VEYGGYASPF AAASHEMRSE MSRRFGTDVA
YAFRHLPSSE PLERHAALAN EAGAEQGRFW EMRDALLSEA PLRDPRQLRR AAAAAGLNLR
RFERDLAAEV GRSRVDEDTS DARAMHLLEA PAFFIDGMRY TGALDADSVN AAVREARDRV
RDATIPARSG GARVGGRRAG LRGGGR
//