TLCE_RICTY
ID TLCE_RICTY Reviewed; 500 AA.
AC Q68W11;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=ADP,ATP carrier protein 5;
DE AltName: Full=ADP/ATP translocase 5;
GN Name=tlcE; Synonyms=tlc5; OrderedLocusNames=RT0724;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
CC -!- FUNCTION: Provides the rickettsial cell with host ATP in exchange for
CC rickettsial ADP. This is an obligate exchange system. This energy
CC acquiring activity is an important component of rickettsial parasitism
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ADP/ATP translocase tlc family.
CC {ECO:0000305}.
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DR EMBL; AE017197; AAU04181.1; -; Genomic_DNA.
DR RefSeq; WP_011191157.1; NC_006142.1.
DR AlphaFoldDB; Q68W11; -.
DR STRING; 257363.RT0724; -.
DR EnsemblBacteria; AAU04181; AAU04181; RT0724.
DR KEGG; rty:RT0724; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; TSKEMLY; -.
DR OrthoDB; 427341at2; -.
DR Proteomes; UP000000604; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR InterPro; IPR004667; ADP_ATP_car_bac_type.
DR PANTHER; PTHR31187; PTHR31187; 1.
DR Pfam; PF03219; TLC; 1.
DR TIGRFAMs; TIGR00769; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..500
FT /note="ADP,ATP carrier protein 5"
FT /id="PRO_0000286480"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 500 AA; 57166 MW; 73F44142C89EDCF9 CRC64;
MLSTSQSRSF KNKFRAAFWP VHNYELGKFI PISALMFCIL FNQNILRILK DSILISEISA
EIAGFAKVYC VTPVAALFVI IYAKMINHLT FEKIFYYLSA FFISCFILFA FVIYPNIHIF
HVHPDTLSDW MNKYPHFKWY ISLVGNWGYI VYYSLAELWP NIFYVLLFWQ FTNELTTTEE
AKRFYTLFSL FGNSSLILVG FLMMNLSSED TIIKKFVSIS DSKITLVQVS TTIVAIVAII
CCLLVRFISK YIFTNPLFYA KIKKSRSTTQ RMGLIKSFKY IAKSKYLWLL LICSAAFGFA
INLVEAVWKA KIKELYPTVN TYAEFNSLYI LWTGVAIIVM TIIGNNVMRM HNWFVAAVIS
PVIIMVTGIL FFVLIVFDQQ ILSLFDGAIL MSPLALAVSI GGIQNILAKG TKYSIWDTSR
EMLYIPLDDE LKTKGKAAVD VISAKIGKSS SGLVQSIIFT LVPNATFTSI SPILMVVFTF
VCFAWIYAVR KIYFEYQKIT