CHAA_ECOLI
ID CHAA_ECOLI Reviewed; 366 AA.
AC P31801;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Sodium-potassium/proton antiporter ChaA {ECO:0000305};
DE AltName: Full=Na(+)/H(+) exchanger;
GN Name=chaA {ECO:0000303|PubMed:8496184}; OrderedLocusNames=b1216, JW1207;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN SODIUM AND CALCIUM EXPORT,
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=NM8191;
RX PubMed=8496184; DOI=10.1016/s0021-9258(18)82124-x;
RA Ivey D.M., Guffanti A.A., Zemsky J., Pinner E., Karpel R., Padan E.,
RA Schuldiner S., Krulwich T.A.;
RT "Cloning and characterization of a putative Ca2+/H+ antiporter gene from
RT Escherichia coli upon functional complementation of Na+/H+ antiporter-
RT deficient strains by the overexpressed gene.";
RL J. Biol. Chem. 268:11296-11303(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN SODIUM AND CALCIUM EXPORT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8021217; DOI=10.1128/jb.176.14.4311-4315.1994;
RA Ohyama T., Igarashi K., Kobayashi H.;
RT "Physiological role of the chaA gene in sodium and calcium circulations at
RT a high pH in Escherichia coli.";
RL J. Bacteriol. 176:4311-4315(1994).
RN [6]
RP FUNCTION IN SODIUM EXPORT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9518629; DOI=10.1016/s0005-2728(97)00102-3;
RA Sakuma T., Yamada N., Saito H., Kakegawa T., Kobayashi H.;
RT "pH dependence of the function of sodium ion extrusion systems in
RT Escherichia coli.";
RL Biochim. Biophys. Acta 1363:231-237(1998).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP FUNCTION IN POTASSIUM EXPORT, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16687400; DOI=10.1074/jbc.m600333200;
RA Radchenko M.V., Tanaka K., Waditee R., Oshimi S., Matsuzaki Y.,
RA Fukuhara M., Kobayashi H., Takabe T., Nakamura T.;
RT "Potassium/proton antiport system of Escherichia coli.";
RL J. Biol. Chem. 281:19822-19829(2006).
RN [9]
RP FUNCTION IN CALCIUM EXPORT.
RC STRAIN=K12;
RX PubMed=18342619; DOI=10.1016/j.bbamem.2008.02.006;
RA Naseem R., Holland I.B., Jacq A., Wann K.T., Campbell A.K.;
RT "pH and monovalent cations regulate cytosolic free Ca(2+) in E. coli.";
RL Biochim. Biophys. Acta 1778:1415-1422(2008).
CC -!- FUNCTION: Sodium exporter that functions mainly at alkaline pH
CC (PubMed:8496184, PubMed:9518629, PubMed:8021217). Can also function as
CC a potassium/proton and calcium/proton antiporter at alkaline pH
CC (PubMed:8496184, PubMed:16687400, PubMed:8021217, PubMed:18342619).
CC Does not play a major role in calcium export (PubMed:18342619). The
CC K(+)/H(+) antiporter activity may enable E.coli to adapt to K(+)
CC salinity stress and to maintain K(+) homeostasis (PubMed:16687400).
CC {ECO:0000269|PubMed:16687400, ECO:0000269|PubMed:18342619,
CC ECO:0000269|PubMed:8021217, ECO:0000269|PubMed:8496184,
CC ECO:0000269|PubMed:9518629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out);
CC Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:8496184};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29420;
CC Evidence={ECO:0000269|PubMed:8496184};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:16687400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29468;
CC Evidence={ECO:0000269|PubMed:16687400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + H(+)(out) = Ca(2+)(out) + H(+)(in);
CC Xref=Rhea:RHEA:71799, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:8496184};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71800;
CC Evidence={ECO:0000269|PubMed:8496184};
CC -!- ACTIVITY REGULATION: Pronounced pH dependence with sodium as substrate
CC (PubMed:8496184). Ca(2+)/H(+) and Na(+)/H(+) antiporter activities are
CC both inhibited by magnesium (PubMed:8496184). Ca(2+)/H(+) activity is
CC inhibited by the proton ionophore carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP) (PubMed:8496184).
CC {ECO:0000269|PubMed:8496184}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. {ECO:0000305}.
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DR EMBL; L28709; AAA20200.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74300.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36074.1; -; Genomic_DNA.
DR PIR; A46716; A46716.
DR RefSeq; NP_415734.1; NC_000913.3.
DR RefSeq; WP_000063607.1; NZ_SSZK01000010.1.
DR AlphaFoldDB; P31801; -.
DR SMR; P31801; -.
DR BioGRID; 4260120; 11.
DR STRING; 511145.b1216; -.
DR TCDB; 2.A.19.1.1; the ca(2+):cation antiporter (caca) family.
DR PaxDb; P31801; -.
DR PRIDE; P31801; -.
DR EnsemblBacteria; AAC74300; AAC74300; b1216.
DR EnsemblBacteria; BAA36074; BAA36074; BAA36074.
DR GeneID; 945790; -.
DR KEGG; ecj:JW1207; -.
DR KEGG; eco:b1216; -.
DR PATRIC; fig|1411691.4.peg.1066; -.
DR EchoBASE; EB1703; -.
DR eggNOG; COG0387; Bacteria.
DR HOGENOM; CLU_050648_0_0_6; -.
DR InParanoid; P31801; -.
DR OMA; AAVMITC; -.
DR PhylomeDB; P31801; -.
DR BioCyc; EcoCyc:CHAA-MON; -.
DR BioCyc; MetaCyc:CHAA-MON; -.
DR PRO; PR:P31801; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IDA:EcoCyc.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:EcoCyc.
DR GO; GO:0010446; P:response to alkaline pH; IDA:EcoCyc.
DR InterPro; IPR004837; NaCa_Exmemb.
DR Pfam; PF01699; Na_Ca_ex; 2.
PE 1: Evidence at protein level;
KW Antiport; Calcium; Cell inner membrane; Cell membrane; Ion transport;
KW Membrane; Potassium; Reference proteome; Sodium; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..366
FT /note="Sodium-potassium/proton antiporter ChaA"
FT /id="PRO_0000209506"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..106
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..167
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..255
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..318
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 366 AA; 39168 MW; C16935AC6A6D811E CRC64;
MSNAQEAVKT RHKETSLIFP VLALVVLFLW GSSQTLPVVI AINLLALIGI LSSAFSVVRH
ADVLAHRLGE PYGSLILSLS VVILEVSLIS ALMATGDAAP TLMRDTLYSI IMIVTGGLVG
FSLLLGGRKF ATQYMNLFGI KQYLIALFPL AIIVLVFPMA LPAANFSTGQ ALLVALISAA
MYGVFLLIQT KTHQSLFVYE HEDDSDDDDP HHGKPSAHSS LWHAIWLIIH LIAVIAVTKM
NASSLETLLD SMNAPVAFTG FLVALLILSP EGLGALKAVL NNQVQRAMNL FFGSVLATIS
LTVPVVTLIA FMTGNELQFA LGAPEMVVMV ASLVLCHISF STGRTNVLNG AAHLALFAAY
LMTIFA
