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