VATI2_TREPA
ID VATI2_TREPA Reviewed; 454 AA.
AC O83544;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=V-type ATP synthase subunit I 2;
DE AltName: Full=V-ATPase subunit I 2;
GN Name=atpI2; OrderedLocusNames=TP_0533;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(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; AE000520; AAC65519.1; -; Genomic_DNA.
DR PIR; F71313; F71313.
DR RefSeq; WP_010881980.1; NC_000919.1.
DR AlphaFoldDB; O83544; -.
DR SMR; O83544; -.
DR IntAct; O83544; 3.
DR STRING; 243276.TPANIC_0533; -.
DR EnsemblBacteria; AAC65519; AAC65519; TP_0533.
DR KEGG; tpa:TP_0533; -.
DR eggNOG; COG1269; Bacteria.
DR HOGENOM; CLU_602593_0_0_12; -.
DR Proteomes; UP000000811; 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.
DR Pfam; PF01496; V_ATPase_I; 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..454
FT /note="V-type ATP synthase subunit I 2"
FT /id="PRO_0000119243"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 101..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 50847 MW; E96C1E95A9C1BD33 CRC64;
MFRSQRMKFL ELVVLERDVD RVLEYLGKTA LVHLRLSAAA RGSSSHCAQS KEYVGRLEEA
CKYLGVSGEC AFSPGDSLPT EEDYTLAQQI LAEVDALHAR EREGDAPSVP RGKSSVAHDS
ANEEQFQGEK CALGSMRGPA LCALLRRFAL QERVHRTRDA LESTRHTYRI AGWLPAHEAK
DLVAGLDNVT TGRMAVRLFE PQELSFIRDG SEHVPVCYQH GRFVRSYERM VSSYGCPPYG
LVDPTPFVAF SYALLFGIMF GDLGQGLLFF VLGLLLRTRR VRALNRWAHL DYVFLSVGFS
SMVMGFLTGE FFAHGTLLAP LIRSVTALCG GVPRDHILHL MPSHGSLHTL MAFFGFTLFL
GFVINSLGLI INIVNQVRLR HALQQCVQKR ECADSSFFGT WLPLQCAYHF LEFHSGSLMR
LQWACLSWVF FVKSFWSVCA SVCVRGFLKV LACI
