MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
Description | RecName: Full=ATP synthase gamma chain {ECO:0000255|HAMAP-Rule:MF_00815}; AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815}; AltName: Full=F-ATPase gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815}; |
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MyHits synonyms | ATPG_STRSV , A3CM13 , 546D2F7A86898485 |
![]() Legends: 1, ipat:ATPASE_GAMMA [T].
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ID ATPG_STRSV Reviewed; 293 AA. AC A3CM13; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 30-NOV-2016, entry version 70. DE RecName: Full=ATP synthase gamma chain {ECO:0000255|HAMAP-Rule:MF_00815}; DE AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815}; DE AltName: Full=F-ATPase gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815}; GN Name=atpG {ECO:0000255|HAMAP-Rule:MF_00815}; GN OrderedLocusNames=SSA_0787; OS Streptococcus sanguinis (strain SK36). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=388919; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK36; RX PubMed=17277061; DOI=10.1128/JB.01808-06; RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., RA Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., RA Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L., RA Buck G.A.; RT "Genome of the opportunistic pathogen Streptococcus sanguinis."; RL J. Bacteriol. 189:3166-3175(2007). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The gamma chain is believed to be CC important in regulating ATPase activity and the flow of protons CC through the CF(0) complex. {ECO:0000255|HAMAP-Rule:MF_00815}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. {ECO:0000255|HAMAP- CC Rule:MF_00815}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00815}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00815}. CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. CC {ECO:0000255|HAMAP-Rule:MF_00815}. DR EMBL; CP000387; ABN44218.1; -; Genomic_DNA. DR RefSeq; WP_002895995.1; NC_009009.1. DR RefSeq; YP_001034768.1; NC_009009.1. DR ProteinModelPortal; A3CM13; -. DR STRING; 388919.SSA_0787; -. DR EnsemblBacteria; ABN44218; ABN44218; SSA_0787. DR GeneID; 4806169; -. DR KEGG; ssa:SSA_0787; -. DR PATRIC; 19768582; VBIStrSan33173_0753. DR eggNOG; ENOG4105J80; Bacteria. DR eggNOG; COG0224; LUCA. DR HOGENOM; HOG000215910; -. DR KO; K02115; -. DR OMA; DRGMCGG; -. DR Proteomes; UP000002148; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR CDD; cd12151; F1-ATPase_gamma; 1. DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1. DR InterPro; IPR000131; ATP_synth_F1_gsu. DR InterPro; IPR023632; ATP_synth_F1_gsu_CS. DR PANTHER; PTHR11693; PTHR11693; 1. DR Pfam; PF00231; ATP-synt; 1. DR PRINTS; PR00126; ATPASEGAMMA. DR SUPFAM; SSF52943; SSF52943; 1. DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1. DR PROSITE; PS00153; ATPASE_GAMMA; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT CHAIN 1 293 ATP synthase gamma chain. FT /FTId=PRO_1000053355. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 278 291 ipat:ATPASE_GAMMA [T] FT MYHIT 4 292 ipfam:ATP-synt [T] FT MYHIT 2 292 ihamap:ATP_synth_gamma_bact [T] SQ SEQUENCE 293 AA; 32541 MW; 546D2F7A86898485 CRC64; MAVSLNDIKN KIASTKNTSQ ITNAMQMVSA AKLGKSEEAA KNFQVYAQKV RKLVTDMLHG HEAENARHHS MLISRPVKKS AYIVITSDRG LVGGYNATIL KALMELKAEY HPTGEDFEVI CIGSVGADFF RARGIQPVYE LRGLADQPSF DEVRKIISKT IEMYQNELFD ELYVCYNHHV NSLTSQMRVE QMLPIIDLDP NEADEDYTLN LELESSRDSI LDQLLPQFAE SMIYGAIIDA KTAENAAGMT AMQTATDNAK KVISDLTIQY NRARQAAITQ EITEIVAGAS ALE // |