ID I3TMK8_TISMK Unreviewed; 909 AA.
AC I3TMK8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=ABC transporter permease ATP-binding protein {ECO:0000313|EMBL:AFK53996.1};
GN Name=yhiH {ECO:0000313|EMBL:AFK53996.1};
GN OrderedLocusNames=TMO_2158 {ECO:0000313|EMBL:AFK53996.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK53996.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK53996.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK53996.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003236; AFK53996.1; -; Genomic_DNA.
DR RefSeq; WP_014745673.1; NC_017956.1.
DR AlphaFoldDB; I3TMK8; -.
DR STRING; 1110502.TMO_2158; -.
DR KEGG; tmo:TMO_2158; -.
DR PATRIC; fig|1110502.3.peg.2222; -.
DR eggNOG; COG0842; Bacteria.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_16_3_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03230; ABC_DR_subfamily_A; 2.
DR Gene3D; 3.40.1710.10; abc type-2 transporter like domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR047651; ABC2_perm_RbbA.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR047817; ABC2_TM_bact-type.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; NF033858; ABC2_perm_RbbA; 1.
DR PANTHER; PTHR43038; ATP-BINDING CASSETTE, SUB-FAMILY H, MEMBER 1; 1.
DR PANTHER; PTHR43038:SF4; RIBOSOME-ASSOCIATED ATPASE; 1.
DR Pfam; PF12698; ABC2_membrane_3; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51012; ABC_TM2; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:AFK53996.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 558..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 764..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..904
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..240
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 270..500
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 679..907
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000259|PROSITE:PS51012"
SQ SEQUENCE 909 AA; 98662 MW; 2C8A3CD67BA667B1 CRC64;
MTAVVRLDRV SLTYGKTRAL DAVTLDLPAG RMIGLIGPDG VGKSSLLSLV SGARAVQAGR
VEVLGGDMAD ARHRRETCPR IAYMPQGLGS NLYATLSVFE NVDFFGRLFG HDRAERARRI
GDLLTSTGLA PFAKRPAGKL SGGMKQKLGL CCALIHDPDL LILDEPTTGV DPLSRRQFWD
LIDRIRADRP GMSVIVATAY MEEAARFDHL VAMDDGRALA TGTPVELLAR TGAPTLDDAF
IALLPEEARH GHQRVVIPPR DAAADGGMAI EAEGLTMRFG DFTAVDHVSF QIPRGEIFGF
LGSNGCGKTT TMKMLTGLLP ASEGRARLFG EEVDPRDIEI RRRVGYMSQA FSLYSELTVR
QNLELHARLF RLPEAEIPGR VRAMAGRFDL DTVMDTLPAA LPLGIRQRLS LAVAMIHGPD
ILILDEPTSG VDPVARDVLW QILAELSRRD GVTIFISTHF MNEAERCDRI SLMHAGRVLV
SDRPDEIRRA QGAATLEEAF VAVLESAGAG GGDAAAPVVS DAGPAATTAV VPRQRRFFDP
RRMLSYTRRE SLELRRDPIR ATLALLGSVL LMFIIGYGIN MDVEDLTFAV LDRDQTTTSR
SYVRDIAGSR YFIERPPITG YADLDRRMRA GEIVLAIEIP PGFGRDVARG RPVEVGAWFD
GAMPQRAETI RGYVQGMHAH WLATRAAEAG TAAADVFTIQ TRYRYNPDVA SLVAMVPAVI
PLLLILIPAM LMALSVVREK ELGSIVNMYV TPVTRFEFLL GKQLPYVALA MLNFLLLTAL
AVFVFGVPLT GSFLTLAAAA LLYVTAATGI GLLISTFMRS QIAAIFGTTV LTILPAVQFS
GLTDPVSSLE GMGAAIGQIY PTTHFILIAR GTFSKALDFQ DLQASFLPLL IAIPVLTVVS
AMLLKKQAR
//
