ID F9ZPH7_ACICS Unreviewed; 784 AA.
AC F9ZPH7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=TRAG family protein {ECO:0000313|EMBL:AEK56821.1};
GN OrderedLocusNames=Atc_0170 {ECO:0000313|EMBL:AEK56821.1};
OS Acidithiobacillus caldus (strain SM-1).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK56821.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK56821.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK56821.1,
RC ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the VirD4/TraG family.
CC {ECO:0000256|ARBA:ARBA00008806}.
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DR EMBL; CP002573; AEK56821.1; -; Genomic_DNA.
DR RefSeq; WP_014002135.1; NC_015850.1.
DR AlphaFoldDB; F9ZPH7; -.
DR STRING; 990288.Atc_0170; -.
DR KEGG; acu:Atc_0170; -.
DR HOGENOM; CLU_012039_0_1_6; -.
DR OrthoDB; 5298505at2; -.
DR Proteomes; UP000006135; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003688; TraG/VirD4.
DR PANTHER; PTHR37937; CONJUGATIVE TRANSFER: DNA TRANSPORT; 1.
DR PANTHER; PTHR37937:SF1; CONJUGATIVE TRANSFER: DNA TRANSPORT; 1.
DR Pfam; PF02534; T4SS-DNA_transf; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006135};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 747..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 87170 MW; 6C18C0E6CC7AC9B0 CRC64;
MPRNTVPALH RPNSEVLDYK TQRIARGGGL KTTLSGIAAG VIGFTLGISY DAREVFPGYQ
WTDDFIQKAH AYLAFDGWRL YNPLPFLRPM LLNLNYPVIH QAFYYAGLPA VTLGVLVAGL
VGFKHKDARQ AVMNNPVHGS AHWATREDAE NAALLPSTGK TRDQKLKYRQ WLKLRRQAAE
QWKRWYRQEH PGKPVPKPII FNKFFEKGVD GQLKDSPHVC YVGAFVEKGK ATPLQHTGAE
HILCFAPTRS GKGVGLVLPT LLDGWMDSVV VHDIKGENFC LTAGYRKSMG HYILRFSPGS
TSDEGCHFNP LDAVRVGTQY EVKDVQNIAT MIVDPDGKGL NDHWQKTGFA LLTSVILHVL
YAMPDKTLRG VAAYLNDPTL ESVDVAFERM MQTVHDPDDQ FGWLDGNNQP TQVHPVIAQS
AREMLNKADN EKSGVISTMM SFLSLYRDPI VAKWTEYSDF KITDLQDADR PVSLYLVTSP
EDKGRLKPLI RLILNQIASQ FTAEERLVAE NGRIKCRGKH RLLLLLDEFP SLGKMDIFQD
SIAFLAGYNV KLYLITQDIA QLEDEGHGYG KAGAKAIIGN CHVRVAYAPN QVETAKWISD
MLGTRTVTLE NDNQSFDGSI LAQQKGYSTS IHYQSRPLLT ADEVMTLRGP VKAGSAIKAP
GDMLIFSAGF PPIYGQQLLY FQNPEWVSRA AIPWPDRSDE LPGARKDYEI VFGPSKGILS
VPKIEKKEGD GGDSLTPETL AALGELDNQL NTLAPSREAA PKGEGKYDTS ERDTEREQVG
RLMG
//
