ID Q2L0U7_BORA1 Unreviewed; 906 AA.
AC Q2L0U7;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:CAJ49423.1};
GN OrderedLocusNames=BAV1814 {ECO:0000313|EMBL:CAJ49423.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49423.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ49423.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ49423.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49423.1; -; Genomic_DNA.
DR RefSeq; WP_012417484.1; NC_010645.1.
DR AlphaFoldDB; Q2L0U7; -.
DR STRING; 360910.BAV1814; -.
DR GeneID; 41393661; -.
DR KEGG; bav:BAV1814; -.
DR eggNOG; COG0842; Bacteria.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_16_3_4; -.
DR OrthoDB; 9776369at2; -.
DR Proteomes; UP000001977; 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; 1.
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:CAJ49423.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 711..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 761..784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..241
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 271..501
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 659..904
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000259|PROSITE:PS51012"
SQ SEQUENCE 906 AA; 99415 MW; 756EEF9E6322CFF2 CRC64;
MSAPVVRLEH VSLHYGKTVA LEDLTQDVPA GLMVGLIGPD GVGKSSLLSL VSGARAVQQG
RVMVLGGDMA DAGHRERVCP RIAYMPQGLG KNLYPTLSVE ENLQFFGRLF GHDASERRRR
IDALTRATGM AAFLDRPAGK LSGGMKQKLG LCCALIHDPD LLVLDEPTTG VDPLARAQFW
DLISEIRQER PGMSVIVATA YMDEAQRFDW LIAMDAGRIL ATGTPADLLA ASQRQTLEEA
FIALLPDEKK RGHQAVKIRP LALDADAETA IEARDLTMRF GDFVAVDHVN FRIRRGEIFG
FLGSNGCGKS TTMKMLTGLL PASEGQAWLF GHEVDPRDID TRRRVGYMSQ AFSLYGELTV
RQNLVLHARL FHVPEADIDQ RVADMAARFD LADVLDVLPE NLPLGVRQRL SLAVAMVHKP
ELLILDEPTS GVDPVARDNF WRLLIALARD DKVTIFISTH FMNEAQRCDR ISLMHAGRVL
VSDTPDAITR QRDAATLEEA FIAYLVEAGA GTTPEQEQAT PDAAPPMPAH TRGFQLGRAI
SYMWRESLEL RRDPVRATLA LVGSLLLMFV MGYGISMDVE DLRYAVLDRD QTSLSQNYAL
NLSGSRYFIE RPPLTDYDDL DQRMRSGELS LAIEIPPGFA RDTQRGAKTQ IGVWIDGAMP
QRAETVRGYV QGMHMGWLLS KAREQGNGAA GMPVDIETRF RYNPDVRSLP AMVPAIIPLL
LLMMPAMLTA LAVVREKELG SIINLYVTPV TRLEFLLSKQ APYVVLAMLN FLLMVLLAVT
VFNVPVTGNL ATLLLAALIY SVISTAIGLL ASTFTRSQIA ALFFTMIGTM VPAVQFAGLI
NPVPSLEGAG RLIGEIYPAT HMLTITRGVF SKALSLPDLY SAFWPLLIAV PIILGASVLL
LKKQES
//
