VATI_CHLMU
ID VATI_CHLMU Reviewed; 649 AA.
AC Q9PK88;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=V-type ATP synthase subunit I;
DE AltName: Full=V-ATPase subunit I;
GN Name=atpI; OrderedLocusNames=TC_0579;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39414.1; -; Genomic_DNA.
DR PIR; C81687; C81687.
DR RefSeq; WP_010230892.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PK88; -.
DR SMR; Q9PK88; -.
DR STRING; 243161.TC_0579; -.
DR EnsemblBacteria; AAF39414; AAF39414; TC_0579.
DR GeneID; 1245938; -.
DR KEGG; cmu:TC_0579; -.
DR eggNOG; COG1269; Bacteria.
DR HOGENOM; CLU_025558_1_1_0; -.
DR OMA; MAVNIMA; -.
DR OrthoDB; 259071at2; -.
DR Proteomes; UP000000800; 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; 2.
PE 3: Inferred from homology;
KW Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..649
FT /note="V-type ATP synthase subunit I"
FT /id="PRO_0000119238"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 649 AA; 73435 MW; 1770AD857A103FC4 CRC64;
MRINVDKYLF IGRKKSEFFS ACRELGAVEF LAKNKLKDSE NVRRISEGLK TLNLLTNKYS
PSDLVLVKSG YLTTEQLLQE IFDLNHEITT ITDSLKALSK EIFRVKPLGN FSSEEIRELT
LKTGLSVRFF YKKHIEGAPL EVEEENVFYL ATAYNYDYYV VIGVVSLSKD IFTEIEAPRS
VGELREEEEH LQTLLRKKKA RVCELYAYRE ELLEALCEQC NEQTLQHAEA STEDLFDDKV
FSALGWVIVD RLTEVEKLCN SLGVYLERVQ PDPDEVIPTY LENHGLGALG ESLVNIYDTP
ASTDKDPSLW VFLSFFVFFS MIINDAGYGL IFLATSLFLS FKARKQVKHS LALKRFLKMF
MILGGGCVCW GGATTSFFGV SVSYTSPFRE YSLTHFLAMK KAEYYLKERP KGYKELVHDY
PVLKDKKTPK EFLLAQGTSS GDSVYKAVVY DKFTDNILME IALLVGVVHL SLGMLRYCRQ
RYSSIGWVVF MCGAYMYLPI YLQAVSLIHY ALHVPYELGG QVGYYVTFIG LGIAVLGGII
QRGLRGLDEV TAVIQVFSDV LSYLRLYALS LAGAMVGNTV MVMSERFSPA VGVLIIIFGH
TVNIALSIMG GVIHGLRLNF IEWYHYSFDG GGRLLHPLKR VICQKSQNI