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NHAA_BIFBU
ID   NHAA_BIFBU              Reviewed;         462 AA.
AC   Q2VPW7; F9XYN2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Bbr_0798;
OS   Bifidobacterium breve (strain NCIMB 8807 / UCC2003).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=326426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 8807 / UCC2003;
RX   PubMed=16321946; DOI=10.1128/jb.187.24.8411-8426.2005;
RA   Ventura M., Zhang Z., Cronin M., Canchaya C., Kenny J.G., Fitzgerald G.F.,
RA   van Sinderen D.;
RT   "The ClgR protein regulates transcription of the clpP operon in
RT   Bifidobacterium breve UCC 2003.";
RL   J. Bacteriol. 187:8411-8426(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 8807 / UCC2003;
RX   PubMed=21690406; DOI=10.1073/pnas.1105380108;
RA   O'Connell Motherway M., Zomer A., Leahy S.C., Reunanen J., Bottacini F.,
RA   Claesson M.J., O'Brien F., Flynn K., Casey P.G., Moreno Munoz J.A.,
RA   Kearney B., Houston A.M., O'Mahony C., Higgins D.G., Shanahan F., Palva A.,
RA   de Vos W.M., Fitzgerald G.F., Ventura M., O'Toole P.W., van Sinderen D.;
RT   "Functional genome analysis of Bifidobacterium breve UCC2003 reveals type
RT   IVb tight adherence (Tad) pili as an essential and conserved host-
RT   colonization factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:11217-11222(2011).
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: Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter
CC       family. {ECO:0000255|HAMAP-Rule:MF_01844}.
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DR   EMBL; AY955251; AAY29675.1; -; Genomic_DNA.
DR   EMBL; CP000303; ABE95483.1; -; Genomic_DNA.
DR   RefSeq; WP_015438691.1; NC_020517.1.
DR   AlphaFoldDB; Q2VPW7; -.
DR   SMR; Q2VPW7; -.
DR   STRING; 326426.Bbr_0798; -.
DR   EnsemblBacteria; ABE95483; ABE95483; Bbr_0798.
DR   KEGG; bbru:Bbr_0798; -.
DR   PATRIC; fig|326426.4.peg.865; -.
DR   eggNOG; COG3004; Bacteria.
DR   HOGENOM; CLU_015803_0_0_11; -.
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   PANTHER; PTHR30341; PTHR30341; 1.
DR   Pfam; PF06965; Na_H_antiport_1; 1.
PE   3: Inferred from homology;
KW   Antiport; Cell membrane; Ion transport; Membrane; Sodium; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..462
FT                   /note="Na(+)/H(+) antiporter NhaA"
FT                   /id="PRO_0000334240"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        256..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01844"
SQ   SEQUENCE   462 AA;  48773 MW;  490852D8B17FFAF0 CRC64;
     MATTTGAKRG IWPMIRRIAA SDRISGLIML GFALAGLVLA NLPLTAHAFE AVAETHVFIP
     HTNLDLPIGH WAQDGLLTIF FLTVGLELKQ ELTTGSLANP KAAAVPMLCA VGGMITPPIL
     FLATTALFSQ FGPGEPGSLI LATTGSSIPF AEMSHGWAVP TATDIAFSLA VLALFAKALP
     GSIRAFLMTL ATVDDLLAII LIAVFFSSVN AWYWFIGIAV CAVVWAHLVR LKKVPWIAVG
     VVGILAWIMM FEAGIHPTLA GVLVGLLTPA RVMHGEYSPR AERYADKLKP FSALLALPIF
     ALFATGVHFE SMSPLLLLSP LVIALIVALV VGKPLGIIVT AWLATHVGGL KMAKGLRVRD
     MIPAAVACGI GFTVSFLIAS LAYTNQELSA EARFGVLVAS LIAAAISGVL LSRQSKRFEQ
     AAAVAAAEAD AESDVNTHSD ELAEHSITLA DGTESVEIDF RR
 
 
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