VATI_BORBU
ID VATI_BORBU Reviewed; 608 AA.
AC O51118;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=V-type ATP synthase subunit I;
DE AltName: Full=V-ATPase subunit I;
GN Name=atpI; OrderedLocusNames=BB_0091;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AE000783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C70111; C70111.
DR RefSeq; WP_023003276.1; NC_001318.1.
DR RefSeq; YP_008686559.1; NC_001318.1.
DR PRIDE; O51118; -.
DR PATRIC; fig|224326.49.peg.489; -.
DR OMA; MAVNIMA; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR PANTHER; PTHR11629; PTHR11629; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..608
FT /note="V-type ATP synthase subunit I"
FT /id="PRO_0000119237"
FT TRANSMEM 308..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 608 AA; 69123 MW; 4B430DF23A521A36 CRC64;
MIVKMKKVLL LTLSKYKKES LEILRDFGAV HINSCNKNSD SLKKSIDDRR ILMQAFSLLK
EDGGVKALKS SNGNFLDIAK SIVNLGNEIK EFQDIKRSLL HERNLISVWG NFSLENIDEL
KESNIYIQFF KIQKSEYKNL LRDPNVNVLL IKNVKNTSYF VSVGEFEQKI EIADEFKFNF
DLDYINNKLK VVDEILDQKL TQISLFNKYI DILRDEIKNY DQIVEFEQVL ADMQTDXEDF
SYITGFVPAE SQESLKNAVL KAGFAAQFAD PEENDIIPTY IKRKGIANLA APIFNILETI
PGYKERDISF IFMLFFFVFF GMIIGDAAYG VIFFLIGILL SLSFLLKGKP LTPFHGLIFY
LSVSSILYGA MTGTWFGSPL ILEMFPILNS FKVSYLTEKN SVQNIIFICF SIGVLQISLA
HVWNFFRQVK EKPHIHSIAQ IGWLMCIVGL YYLVLNLILS QSRFPMYNVV YNVIYFGVAL
VFVFGKQDGS NFFKCILKSF GGIIEQFLTT VSGFADIISY IRLFAVGLAG LSISASFNTM
SIPLLKSSNI GLIVAGIIVI LFGHVLNIML SLLSVIVHGV RLNMLEFSNH LGQEWSGCAY
RPFKKMKK