Tag | Content |
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CPLM ID | CPLM-013485 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | V-type ATP synthase beta chain |
Protein Synonyms/Alias | V-ATPase subunit B |
Gene Name | atpB |
Gene Synonyms/Alias | TTHA1272 |
Created Date | July 27, 2013 |
Organism | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
NCBI Taxa ID | 300852 |
Lysine Modification | Position | Peptide | Type | References |
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86 | VARLGVSKEMLGRRF | acetylation | [1] |
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Reference | [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus. Okanishi H, Kim K, Masui R, Kuramitsu S. J Proteome Res. 2013 Aug 1;. [ PMID: 23901841] |
Functional Description | Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit. |
Sequence Annotation | |
Keyword | 3D-structure; ATP synthesis; Complete proteome; Hydrogen ion transport; Ion transport; Reference proteome; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 478 AA |
Protein Sequence | MDLLKKEYTG ITYISGPLLF VENAKDLAYG AIVDIKDGTG RVRGGQVIEV SEEYAVIQVF 60 EETTGLDLAT TSVSLVEDVA RLGVSKEMLG RRFNGIGKPI DGLPPITPEK RLPITGLPLN 120 PVARRKPEQF IQTGISTIDV MNTLVRGQKL PIFSGSGLPA NEIAAQIARQ ATVRPDLSGE 180 GEKEEPFAVV FAAMGITQRE LSYFIQEFER TGALSRSVLF LNKADDPTIE RILTPRMALT 240 VAEYLAFEHD YHVLVILTDM TNYCEALREI GAAREEIPGR RGYPGYMYTD LATIYERAGV 300 VEGKKGSVTQ IPILSMPDDD RTHPIPDLTG YITEGQIQLS RELHRKGIYP PIDPLPSLSR 360 LMNNGVGKGK TREDHKQVSD QLYSAYANGV DIRKLVAIIG EDALTENDRR YLQFADAFER 420 FFINQGQQNR SIEESLQIAW ALLSMLPQGE LKRISKDHIG KYYGQKLEEI WGAPQALD 478 |
Gene Ontology | GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:HAMAP. GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |