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NHAA_HERAR
ID   NHAA_HERAR              Reviewed;         621 AA.
AC   A4G6P0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Na(+)/H(+) antiporter NhaA {ECO:0000255|HAMAP-Rule:MF_01844};
DE   AltName: Full=Sodium/proton antiporter NhaA {ECO:0000255|HAMAP-Rule:MF_01844};
GN   Name=nhaA {ECO:0000255|HAMAP-Rule:MF_01844}; OrderedLocusNames=HEAR2033;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
CC   -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC       external protons. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01844};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29252;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01844};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01844}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01844}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NhaA Na(+)/H(+)
CC       (TC 2.A.33) antiporter family. {ECO:0000305}.
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DR   EMBL; CU207211; CAL62177.1; -; Genomic_DNA.
DR   RefSeq; WP_011871462.1; NC_009138.1.
DR   AlphaFoldDB; A4G6P0; -.
DR   SMR; A4G6P0; -.
DR   STRING; 204773.HEAR2033; -.
DR   EnsemblBacteria; CAL62177; CAL62177; HEAR2033.
DR   KEGG; har:HEAR2033; -.
DR   eggNOG; COG1651; Bacteria.
DR   eggNOG; COG3004; Bacteria.
DR   HOGENOM; CLU_015803_3_0_4; -.
DR   OMA; TFFFFIV; -.
DR   OrthoDB; 1805428at2; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 1.20.1530.10; -; 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   PANTHER; PTHR30341; PTHR30341; 1.
DR   Pfam; PF06965; Na_H_antiport_1; 1.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00773; NhaA; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW   Reference proteome; Sodium; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..621
FT                   /note="Na(+)/H(+) antiporter NhaA"
FT                   /id="PRO_0000334477"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   DOMAIN          431..578
FT                   /note="Thioredoxin"
FT   REGION          1..430
FT                   /note="Na(+)/H(+) antiporter NhaA"
SQ   SEQUENCE   621 AA;  67096 MW;  FEB3397F95720FB9 CRC64;
     MPASSFGESS AHIRRRRVAH YLRTESGAAV LLVIVTVVAL VWANSPLSNA YFELWHLDVG
     FNFGPLRLHM DLHHWVNDGL MVVFFFLIGL EVRQEFAHGS LRDRSRARLA LIAGVTGVVL
     PALVYVLIVK LAGSEGLHGW GAVVGTDTAF MLGTLAIVGP RLSGQLRVFL LTLTVVDDFL
     AVSIIGIVYS EEIRIVPLLI ALASLVGLWL LGRTRQWRAT PYVLIVIVLW FATVYSGIHA
     SLAGMAAGLL IPAYATQRHG VVAARQLFRD FWQSPSAASA RAVDCGLSRG ISVNERLHEF
     LRLPTALLIV PIFALANAGV DVRGGLLAEA FGSPVTWGVI AGLVLGKLLG IGLTTLVAVR
     LGLGRLPEGV GVGSVFGGAA LSGIGFTVSL LIIGLAFGTT SDLGRQATVG VLVSMVFATL
     LGWLIFKVAA QRWGEKTADL PMVLEPPVDP EIDHIRGPED AQLTLVEYVD FECAYCAHAT
     GSWDDLRAHF GDDLRYVVRH LPHHPHGPIA ARASEAAANQ GMFWPWLDFV FTRQHALERE
     HLIGYAAELG LDVERFIADL DSPAVIERVE RDLASAVASG AHATPTFFVE GRRLRGSYDA
     RTVTAVLEAS RRGTRTQEVP S
 
 
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