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NHAS1_SYNY3
ID   NHAS1_SYNY3             Reviewed;         527 AA.
AC   P73863;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Low-affinity Na(+)/H(+) antiporter NhaS1;
DE   AltName: Full=Sodium/proton antiporter NhaS1;
GN   Name=nhaS1; OrderedLocusNames=slr1727;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND GENE NAME.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=11157951; DOI=10.1128/jb.183.4.1376-1384.2001;
RA   Inaba M., Sakamoto A., Murata N.;
RT   "Functional expression in Escherichia coli of low-affinity and high-
RT   affinity Na(+)(Li(+))/H(+) antiporters of Synechocystis.";
RL   J. Bacteriol. 183:1376-1384(2001).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=11996656; DOI=10.1023/a:1015281906254;
RA   Elanskaya I.V., Karandashova I.V., Bogachev A.V., Hagemann M.;
RT   "Functional analysis of the Na+/H+ antiporter encoding genes of the
RT   cyanobacterium Synechocystis PCC 6803.";
RL   Biochemistry (Mosc.) 67:432-440(2002).
CC   -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC       external protons. Might be able to function at relatively high
CC       concentrations of Na(+) ions. Has also Li(+)/H(+) antiport activity
CC       under K(+)-rich conditions, but it might not have any physiological
CC       relevance. {ECO:0000269|PubMed:11157951, ECO:0000269|PubMed:11996656}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.7 mM for Na(+) (under K(+)-free conditions)
CC         {ECO:0000269|PubMed:11157951};
CC         KM=2.5 mM for Li(+) (under K(+)-free conditions)
CC         {ECO:0000269|PubMed:11157951};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC       transporter (TC 2.A.36) family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA17925.1; -; Genomic_DNA.
DR   PIR; S75063; S75063.
DR   AlphaFoldDB; P73863; -.
DR   IntAct; P73863; 4.
DR   STRING; 1148.1653008; -.
DR   TCDB; 2.A.36.7.2; the monovalent cation:proton antiporter-1 (cpa1) family.
DR   PaxDb; P73863; -.
DR   EnsemblBacteria; BAA17925; BAA17925; BAA17925.
DR   KEGG; syn:slr1727; -.
DR   eggNOG; COG0025; Bacteria.
DR   InParanoid; P73863; -.
DR   OMA; AGMMMNY; -.
DR   PhylomeDB; P73863; -.
DR   SABIO-RK; P73863; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR   GO; GO:0015385; F:sodium:proton antiporter activity; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   GO; GO:0098719; P:sodium ion import across plasma membrane; IBA:GO_Central.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR004705; Cation/H_exchanger_CPA1_bac.
DR   PANTHER; PTHR10110; PTHR10110; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   TIGRFAMs; TIGR00831; a_cpa1; 1.
PE   1: Evidence at protein level;
KW   Antiport; Cell membrane; Ion transport; Membrane; Reference proteome;
KW   Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..527
FT                   /note="Low-affinity Na(+)/H(+) antiporter NhaS1"
FT                   /id="PRO_0000423927"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   527 AA;  57539 MW;  499A0FEFACC4EB0E CRC64;
     MDTAVNESLS ISYNLEQFLI VLSVSLSIAT LSKTVPILRK IPYTLLLVIV GMALAFVDVK
     LINLSPELIM EIFLPPLLFE AAWNLQWRNL KENWFPITLF ATLGVVICVV GIAFPLSYWG
     GMELAIAFLA AAALSATDPV SVIALFKELG ASKKLNTLME GESLFNDGVA VVVFLILVGI
     PLGTSTFDLS VTLARFVTVI GIGVGCGLVI GFSLSLLTQR FDLPFVEQSL TLVSAYGAYI
     LAENLGGSGV IGVVVVGMVL GNYGSRIGMN PRTRLIVSIF WEFVAFFVNS IIFLLIGDQI
     GLSSLSDHLN LILIAIAAVV VTRLVSVFGL SLISNKVSDQ ISSTHITLQE QTVLWWGGLR
     GSVAIAVALS VPQAIAERQA IIDIVFGVVL FTLLVQGLTT QFVLKGLDLI GDQPQRLEYA
     ELVSRQIALR RVLAELEKTD EFPDINPERL RYKQELVQGQ LQSVTDKLKL LLQEYPLLQE
     VANKKFDQTV LDIEAETYAD LIRMGRLEEN IMPLLVTLEG ENVAEPS
 
 
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