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Y043_BIFLO
ID   Y043_BIFLO              Reviewed;         780 AA.
AC   Q8G838;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Putative ABC transporter ATP-binding protein BL0043;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=BL0043;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC   -!- FUNCTION: Probably part of an ABC transporter complex. Responsible for
CC       energy coupling to the transport system (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   -!- CAUTION: The fusion between the ATP-binding domains and one of the
CC       transmembrane domain is unusual. It could be due to a sequencing error.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN23910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014295; AAN23910.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_695274.1; NC_004307.2.
DR   AlphaFoldDB; Q8G838; -.
DR   SMR; Q8G838; -.
DR   STRING; 206672.BL0043; -.
DR   EnsemblBacteria; AAN23910; AAN23910; BL0043.
DR   KEGG; blo:BL0043; -.
DR   PATRIC; fig|206672.9.peg.45; -.
DR   HOGENOM; CLU_000604_38_1_11; -.
DR   OMA; RTHWRVM; -.
DR   Proteomes; UP000000439; 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:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF02361; CbiQ; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..780
FT                   /note="Putative ABC transporter ATP-binding protein BL0043"
FT                   /id="PRO_0000091991"
FT   TRANSMEM        551..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        586..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        623..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        759..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2..238
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          282..531
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          230..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         316..323
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   780 AA;  83262 MW;  DC9724D2760C6B5A CRC64;
     MLKDIRFSYD RGTSWALDGV SLTVHAGERL CLVGPNGSGK STLARLIAGL TAPDGGEVTL
     LGQRVYAAGP NADAYRAARH GIGMVFQNPE DQLVTTVLED DVAFGPENLG LERELIGERI
     VDSLQAVGLA NLRQSDPTRM SGGQQQRASI AGMLAMNPAM LVLDEPTAML DESARAEVMR
     ILDDLQARGT TIVHVTHHPD ETVHADRIVH MEAGRIIGIT AAVDNRSPLA EAVSQSETEG
     SIGTEAAPSR PTNDSPRQRE REDGSELPLL SDGIGDMTNP IIRVSHLTYR YPSAKRAVID
     DLSFTIARGE TVALMGVNGS GKSTLVRMLC ALTAPTAGSI EVAGVPVAST GKRGRNVRPK
     SANRKQLAQL RRHVGYVMQH PEHQLFADTV AEDVAYGPRN QGLGETEVAD RVRESLELLH
     IGHLADRSPF DLSGGQQRLA AIAGVLACNP DVLIMDEPTA SLDAQAKKRI HELLRTLKSR
     GVTVLIITHD REEAEQIADR VVRMPIAAPA SGGPVTATVT EPAVSSNGPA HSVIHRLDPR
     VKMVGFLAAM FTMFAVNTPT QLALGIAITL AVIAAARLNP LRVLESIHPI LILLVLMGVV
     NLFVVRTGTP VVALGPLSIT DQGVTIAVLY ACRFALVIIL GAVFLTTTTP TAMTDAFATL
     ISPLNRLGIH AQEIALVMSL ALRFIPTLTD ETRAIVDAQS ARGGSIETGS LAQRIKAMSA
     IIVPIFAGTL RHADNLSLAL DARCYEEGIR RTHWRALTIA ARDLIFAAAV IIYIAAIIAL
 
 
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