VATI_CHLTR
ID VATI_CHLTR Reviewed; 649 AA.
AC O84307;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=V-type ATP synthase subunit I;
DE AltName: Full=V-ATPase subunit I;
GN Name=atpI; OrderedLocusNames=CT_305;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67898.1; -; Genomic_DNA.
DR PIR; G71530; G71530.
DR RefSeq; NP_219810.1; NC_000117.1.
DR RefSeq; WP_010725153.1; NC_000117.1.
DR AlphaFoldDB; O84307; -.
DR STRING; 813.O172_01635; -.
DR PRIDE; O84307; -.
DR EnsemblBacteria; AAC67898; AAC67898; CT_305.
DR GeneID; 884819; -.
DR KEGG; ctr:CT_305; -.
DR PATRIC; fig|272561.5.peg.326; -.
DR HOGENOM; CLU_025558_1_1_0; -.
DR InParanoid; O84307; -.
DR OMA; MAVNIMA; -.
DR Proteomes; UP000000431; 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:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
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..649
FT /note="V-type ATP synthase subunit I"
FT /id="PRO_0000119240"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
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; 73214 MW; 1D3FC48CF49850FB CRC64;
MRVDVDKYLF IGREKSEFFS ACREIGAVEF LSKSKLKDSE KVRKLSEGLK VLNLLTKSCS
PADLVSTKSG YLVTEQLLQE IFDLNQEITT LTESLKALGK EIVRVKPLGD FSSEEIRELT
LKTGLAVRFL YKRHIEGAPL EVEEENVFYL ATAYNYDYYA VIGIVSLSKD IFTEIEAPRS
VNELREEEGH LQALLRKKKA RVCELYAYRE DLLEALCEQC NEQSLQHAEV SAEDLFDDKV
FSALGWVIVD RLDEVKKLCD SLGIYLERVQ PDPDEVIPTY LENHGLGALG ESLVNIYDTP
ASTDKDPSLW VFFSFFVFFS MIINDAGYGL VFLATSLFLS FKARKQIKRS IALKRFLQMF
MILGLGCVCW GGATTSFFGV SVSYTSPFRE YSLTHFLALK KAEYYLKERP KGYKELVHDY
PILKEKKTPK EFLLAQSTSS GDSVYKAVVY DKFIDNILME IALLVGVVHL SLGMLRYCRQ
RYSSIGWVIF MCGAYMYLPI YLQAVSLIHY ALHIPYELGG LVGYYVAFIG LGVAILGGVI
QRGLRGLDEI TAVIQVFSDV LSYLRLYALS LAGAMVGNTV MVMSERFSPA VGILIIIFGH
TVNIALSIMG GVIHGLRLNF IEWYHYSFDG GGKLLHPLKK VICQKSQNL