ID ATP6_PSEPU STANDARD; PRT; 153 AA. AC P25761; DT 01-MAY-1992 (REL. 22, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE ATP SYNTHASE A CHAIN (EC 3.6.1.34) (PROTEIN 6) (FRAGMENT). GN ATPB OR UNCB. OS PSEUDOMONAS PUTIDA. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC PSEUDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=TN2100; RX MEDLINE; 92204018. RA OGASAWARA N., YOSHIKAWA H.; RL MOL. MICROBIOL. 6:629-634(1992). CC -!- FUNCTION: KEY COMPONENT OF THE PROTON CHANNEL; IT MAY PLAY A CC DIRECT ROLE IN THE TRANSLOCATION OF PROTONS ACROSS THE MEMBRANE. 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. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CONTAINS 8 CC POTENTIAL TRANSMEMBRANE DOMAINS. CC -!- SIMILARITY: BELONGS TO THE ATPASE A CHAIN FAMILY. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X62540; G45716; -. DR PIR; JQ1226; JQ1226. DR PROSITE; PS00449; ATPASE_A. KW HYDROGEN ION TRANSPORT; CF(0); TRANSMEMBRANE. FT NON_TER 153 153 SQ SEQUENCE 153 AA; 16607 MW; 5F153F06 CRC32; MAAETASGYI QHHLQNLTYG QLPDGSWGFA HSAAEAKAMG FWAFHLDTLG WSVALGLIFL LIFRMAAKKA TSGQPGGLQN FVEVMVDFVN GSVKDSFHGR SPVIAPLALT IFVWVFLMNA VDLIPVDWIP QLAILISGDP HIPFRAVSTT DPN //