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NHAA1_RHOJR
ID   NHAA1_RHOJR             Reviewed;         622 AA.
AC   Q0SG15;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Na(+)/H(+) antiporter NhaA 1 {ECO:0000255|HAMAP-Rule:MF_01844};
DE   AltName: Full=Sodium/proton antiporter NhaA 1 {ECO:0000255|HAMAP-Rule:MF_01844};
GN   Name=nhaA1 {ECO:0000255|HAMAP-Rule:MF_01844};
GN   OrderedLocusNames=RHA1_ro01708;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01844};
CC       Multi-pass membrane protein {ECO:0000255|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:0000305}.
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DR   EMBL; CP000431; ABG93521.1; -; Genomic_DNA.
DR   RefSeq; WP_011594648.1; NC_008268.1.
DR   AlphaFoldDB; Q0SG15; -.
DR   SMR; Q0SG15; -.
DR   STRING; 101510.RHA1_ro01708; -.
DR   EnsemblBacteria; ABG93521; ABG93521; RHA1_ro01708.
DR   KEGG; rha:RHA1_ro01708; -.
DR   PATRIC; fig|101510.16.peg.1730; -.
DR   eggNOG; COG1651; Bacteria.
DR   eggNOG; COG3004; Bacteria.
DR   HOGENOM; CLU_015803_3_0_11; -.
DR   OMA; TFFFFIV; -.
DR   Proteomes; UP000008710; 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 membrane; Ion transport; Membrane; Reference proteome;
KW   Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..622
FT                   /note="Na(+)/H(+) antiporter NhaA 1"
FT                   /id="PRO_0000334485"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        73..93
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        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        215..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   DOMAIN          430..617
FT                   /note="Thioredoxin"
FT   REGION          1..429
FT                   /note="Na(+)/H(+) antiporter NhaA"
SQ   SEQUENCE   622 AA;  67068 MW;  8A6CD0F750AED50F CRC64;
     MTVEQSSPTT LRRLSARLAL IRDDTDDDKL SAGFLLVATI LALVWANIGD SYESFWHTPV
     TIQISDNSIS LDLKHWVNDG LMTLFFFVVG LEVKRELTIG ELTDRARAAV PLLAAIAGLA
     LPAVLFLILN PSGDEATAWG VVVSTDTAFV LGALALVGPR CPARLRVFIL TLAVADDIGA
     LALIAFFYTD DLRLGPLLLG CVGLLLIIQL RKLEVWRGVA YFIVAAGTWV AFYESGVHPT
     LVGVLIALIL PVYPPRRSEV ERAGELTRAF RQSPNSDYAR AAQLGVLRAV SVNERLLRFY
     QPYTAFLVVP IFALANAGVV ITGQTLADAA RSPLAWGIVL GLVVGKLVGI TAATALFSKL
     RPGSLPPGLT LSQIAGGSAL AGIGFTISLF IVDLAIDSPE LANEARVGVL TAAVIATVLG
     WALFRLSDTV HPPTEVVGLT LLRPVDPGRD HLRGPADAPL TLVEYGDFEC PFCSKATGSI
     RDVRAHFGDE LRYVFRHLPL DDVHPHARFA AQASEAAAAQ GRFWEMHDHL FANSDALAED
     EIFGYAAELG LDMDRFEEDI RRGTYVHRID DDELDAESSD FRGTPTFYLG ATGTDLARHS
     GPYDAATLIR KLEEARGADG AP
 
 
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