Y796_METJA
ID Y796_METJA Reviewed; 235 AA.
AC Q58206;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ0796;
GN OrderedLocusNames=MJ0796;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=11402022; DOI=10.1074/jbc.m100758200;
RA Yuan Y.-R., Blecker S., Martsinkevich O., Millen L., Thomas P.J.,
RA Hunt J.F.;
RT "The crystal structure of the MJ0796 ATP-binding cassette. Implications for
RT the structural consequences of ATP hydrolysis in the active site of an ABC
RT transporter.";
RL J. Biol. Chem. 276:32313-32321(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT GLN-171.
RX PubMed=12150914; DOI=10.1016/s1097-2765(02)00576-2;
RA Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., Thomas P.J.,
RA Hunt J.F.;
RT "ATP binding to the motor domain from an ABC transporter drives formation
RT of a nucleotide sandwich dimer.";
RL Mol. Cell 10:139-149(2002).
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB98791.1; -; Genomic_DNA.
DR PIR; D64399; D64399.
DR RefSeq; WP_010870305.1; NC_000909.1.
DR PDB; 1F3O; X-ray; 2.70 A; A=1-235.
DR PDB; 1L2T; X-ray; 1.90 A; A/B=1-235.
DR PDB; 3TIF; X-ray; 1.80 A; A/B=1-235.
DR PDBsum; 1F3O; -.
DR PDBsum; 1L2T; -.
DR PDBsum; 3TIF; -.
DR AlphaFoldDB; Q58206; -.
DR SMR; Q58206; -.
DR STRING; 243232.MJ_0796; -.
DR TCDB; 3.A.1.122.14; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAB98791; AAB98791; MJ_0796.
DR GeneID; 1451677; -.
DR KEGG; mja:MJ_0796; -.
DR eggNOG; arCOG00922; Archaea.
DR HOGENOM; CLU_000604_1_22_2; -.
DR InParanoid; Q58206; -.
DR OMA; EFIYIIG; -.
DR OrthoDB; 67630at2157; -.
DR PhylomeDB; Q58206; -.
DR EvolutionaryTrace; Q58206; -.
DR PRO; PR:Q58206; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR017911; MacB_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transport.
FT CHAIN 1..235
FT /note="Uncharacterized ABC transporter ATP-binding protein
FT MJ0796"
FT /id="PRO_0000093221"
FT DOMAIN 2..235
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 16..28
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:3TIF"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 178..195
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:3TIF"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:3TIF"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:3TIF"
SQ SEQUENCE 235 AA; 26566 MW; C3035AE896099E72 CRC64;
MIKLKNVTKT YKMGEEIIYA LKNVNLNIKE GEFVSIMGPS GSGKSTMLNI IGCLDKPTEG
EVYIDNIKTN DLDDDELTKI RRDKIGFVFQ QFNLIPLLTA LENVELPLIF KYRGAMSGEE
RRKRALECLK MAELEERFAN HKPNQLSGGQ QQRVAIARAL ANNPPIILAD EPTGALDSKT
GEKIMQLLKK LNEEDGKTVV VVTHDINVAR FGERIIYLKD GEVEREEKLR GFDDR