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CHAA_BACSU
ID   CHAA_BACSU              Reviewed;         351 AA.
AC   O34840; Q79EY2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Ca(2+)/H(+) antiporter ChaA;
GN   Name=chaA; Synonyms=yfkE; OrderedLocusNames=BSU07920;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / AC327;
RX   PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA   Yamamoto H., Uchiyama S., Sekiguchi J.;
RT   "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT   region of the Bacillus subtilis chromosome containing genes for trehalose
RT   metabolism and acetoin utilization.";
RL   Microbiology 142:3057-3065(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND GENE NAME.
RC   STRAIN=168;
RX   PubMed=19543710; DOI=10.1007/s00203-009-0494-7;
RA   Fujisawa M., Wada Y., Tsuchiya T., Ito M.;
RT   "Characterization of Bacillus subtilis YfkE (ChaA): a calcium-specific
RT   Ca2+/H+ antiporter of the CaCA family.";
RL   Arch. Microbiol. 191:649-657(2009).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), ACTIVITY REGULATION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-64; GLY-68; ASN-69; GLU-72;
RP   ASN-99; LYS-116; ASN-252; GLU-255; HIS-256; SER-258; SER-278 AND GLN-281.
RX   PubMed=23798403; DOI=10.1073/pnas.1302515110;
RA   Wu M., Tong S., Waltersperger S., Diederichs K., Wang M., Zheng L.;
RT   "Crystal structure of Ca2+/H+ antiporter protein YfkE reveals the
RT   mechanisms of Ca2+ efflux and its pH regulation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:11367-11372(2013).
CC   -!- FUNCTION: Ca(+)/H(+) antiporter that extrudes calcium in exchange for
CC       external protons. Does not transport sodium or potassium.
CC       {ECO:0000269|PubMed:19543710}.
CC   -!- ACTIVITY REGULATION: Calcium efflux is tightly regulated by
CC       intracellular pH. {ECO:0000269|PubMed:23798403}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.5 uM for Ca(2+) (at pH 8.5) {ECO:0000269|PubMed:19543710};
CC         KM=37.5 uM for Ca(2+) (at pH 8.0) {ECO:0000269|PubMed:19543710};
CC         KM=113 uM for Ca(2+) (at pH 7.5) {ECO:0000269|PubMed:19543710};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:23798403}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23798403};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:23798403}.
CC   -!- INDUCTION: Transcriptionally regulated by the forespore-specific sigma
CC       factor, SigG, and the general stress response regulator, SigB.
CC       {ECO:0000269|PubMed:19543710}.
CC   -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC       family. Cation/proton exchanger (CAX) subfamily. {ECO:0000305}.
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DR   EMBL; D83967; BAA23395.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12621.1; -; Genomic_DNA.
DR   PIR; A69808; A69808.
DR   RefSeq; NP_388673.1; NC_000964.3.
DR   RefSeq; WP_003242902.1; NZ_JNCM01000032.1.
DR   PDB; 4KJR; X-ray; 3.00 A; A/B=1-351.
DR   PDB; 4KJS; X-ray; 3.05 A; A/B=1-351.
DR   PDBsum; 4KJR; -.
DR   PDBsum; 4KJS; -.
DR   AlphaFoldDB; O34840; -.
DR   SMR; O34840; -.
DR   STRING; 224308.BSU07920; -.
DR   TCDB; 2.A.19.2.11; the ca(2+):cation antiporter (caca) family.
DR   TCDB; 2.A.19.2.7; the ca(2+):cation antiporter (caca) family.
DR   PaxDb; O34840; -.
DR   EnsemblBacteria; CAB12621; CAB12621; BSU_07920.
DR   GeneID; 939693; -.
DR   KEGG; bsu:BSU07920; -.
DR   PATRIC; fig|224308.179.peg.858; -.
DR   eggNOG; COG0387; Bacteria.
DR   InParanoid; O34840; -.
DR   OMA; AAVMITC; -.
DR   PhylomeDB; O34840; -.
DR   BioCyc; BSUB:BSU07920-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015369; F:calcium:proton antiporter activity; IDA:UniProtKB.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR   Gene3D; 1.20.1420.30; -; 1.
DR   InterPro; IPR004713; CaH_exchang.
DR   InterPro; IPR004798; CAX-like.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR   PANTHER; PTHR31503; PTHR31503; 1.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   TIGRFAMs; TIGR00378; cax; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiport; Calcium; Calcium transport; Cell membrane;
KW   Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..351
FT                   /note="Ca(2+)/H(+) antiporter ChaA"
FT                   /id="PRO_0000376844"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         64
FT                   /note="N->A: Almost no change in activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         68
FT                   /note="G->A: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         69
FT                   /note="N->A: Almost loss of activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         72
FT                   /note="E->A: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         99
FT                   /note="N->A: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         116
FT                   /note="K->A: Almost no change in activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         252
FT                   /note="N->A: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         255
FT                   /note="E->A: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         256
FT                   /note="H->A: Almost loss of activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         258
FT                   /note="S->A: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         278
FT                   /note="S->A: Almost no change in activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   MUTAGEN         281
FT                   /note="Q->A: Almost loss of activity."
FT                   /evidence="ECO:0000269|PubMed:23798403"
FT   HELIX           3..22
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           26..53
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           60..66
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           85..99
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           102..110
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:4KJS"
FT   HELIX           121..139
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           141..146
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           152..176
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           204..212
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           216..234
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           239..244
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           246..256
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           258..261
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   STRAND          263..266
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           269..284
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           286..296
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:4KJS"
FT   HELIX           307..324
FT                   /evidence="ECO:0007829|PDB:4KJR"
FT   HELIX           333..350
FT                   /evidence="ECO:0007829|PDB:4KJR"
SQ   SEQUENCE   351 AA;  37522 MW;  D81E4C5FE6081767 CRC64;
     MNRIFFILVA AGVPLSVIGS LMHWPSAVLF AVYCVTIIAL ASYMGRATES LSIIAGPRIG
     GLLNATFGNA VELIISLFAL KEGLTGIVLA SLTGSVLGNL LLVAGLSFFV GGLKYKRQEF
     NIHDARHNSG LLIFAIIVAF VIPEVFSVGM GNASKLNLSI GISIIMILLY VAALYFKLVT
     HRGVYQPNNA AQTEEEEEPE WSGKVATIVL FAATIVVAYI SENLVHTFHS VAEQFGWSEL
     FIGVIIVAIV GNAAEHASAI IMAFKNKMDI AVEIAVGSTL QIAMFVAPVL VICSIFFPTS
     MPLVFTLPEL VAMVSAVLLM IAISNDGDSN WFEGATLLAA YVIMAIGFFL L
 
 
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