ID K4IJW6_BIFAP Unreviewed; 679 AA.
AC K4IJW6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Putative ABC transporter {ECO:0000313|EMBL:AFU70639.1};
DE EC=3.6.3.42 {ECO:0000313|EMBL:AFU70639.1};
GN OrderedLocusNames=BAST_0034 {ECO:0000313|EMBL:AFU70639.1};
OS Bifidobacterium asteroides (strain PRL2011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU70639.1, ECO:0000313|Proteomes:UP000007006};
RN [1] {ECO:0000313|EMBL:AFU70639.1, ECO:0000313|Proteomes:UP000007006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRL2011 {ECO:0000313|EMBL:AFU70639.1,
RC ECO:0000313|Proteomes:UP000007006};
RX PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA Ventura M.;
RT "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT colonization of the insect gut.";
RL PLoS ONE 7:E44229-E44229(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003325; AFU70639.1; -; Genomic_DNA.
DR AlphaFoldDB; K4IJW6; -.
DR STRING; 1147128.BAST_0034; -.
DR KEGG; bast:BAST_0034; -.
DR PATRIC; fig|1147128.3.peg.34; -.
DR eggNOG; COG4988; Bacteria.
DR HOGENOM; CLU_000604_84_9_11; -.
DR Proteomes; UP000007006; Chromosome.
DR GO; GO:0016020; C: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 Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:AFU70639.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..240
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 438..671
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 324..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 71345 MW; 8F60428B2E95A24F CRC64;
MISKRLLHLP GARMGASLLL ALLQTIGALA EVLLLPVAVA AVGRSLGLAV PHALAWVPNR
PGPLAVLIGG LILVWFLTQA VARSVSARLA DGMGKALSQA LYLSVFDPNR QEDDLGVPAQ
TLARLSTEGV KSVVSYFTAY IPALVQTALM LVIALAVLLP VSPLAAVIVV IGMVALPLAS
KPTMGENIKV QLGQLRKYDK VGVHFEHALR GLNTLKIFGA DQRQADDLAE ESEGFRRITM
GVLGGQLRSL IKADVVIYTS LILAVAATVL IGQDGPSRVL SCLVVALAGV RLFAPERQLV
YMMHSGMVAI KQGKAIDDIL QARQGSDGES AAPGTTPESR KKVAPEEVPA TIPEASEEAA
PEVGLEASEE AIQESESESA SKPALQPASE SALEPVSDAV QILAPGSANA MRQNTGSARS
SSQQADQTDM SGDDLPGISA RNLTYTYPDG FQALTNLNFV LPAKGHVGLV GASGSGKSTL
AGLLSGRLQG YAGELTIGGR QISDLSRQDL VGLQTVVRGT DHLFTGTIRS NLDPAGLGYS
DWELLDALDQ VGLTGLVQSK GGLDAHIDPE GGNLSGGQRQ RLSIARGLLR RSPVYIFDEA
TSAVDREHDA TLAALMDALG KESLVLTITH RLAGVRNTDS ILFLQEGRLV ESGGFRELMD
AGGGFAAQWK EQAQYEDGE
//
