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Database: UniProt
Entry: A0A163X9E6_9BRAD
LinkDB: A0A163X9E6_9BRAD
Original site: A0A163X9E6_9BRAD 
ID   A0A163X9E6_9BRAD        Unreviewed;       600 AA.
AC   A0A163X9E6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:KZD20600.1};
GN   ORFNames=A4A58_17835 {ECO:0000313|EMBL:KZD20600.1};
OS   Tardiphaga robiniae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Tardiphaga.
OX   NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD20600.1, ECO:0000313|Proteomes:UP000076574};
RN   [1] {ECO:0000313|EMBL:KZD20600.1, ECO:0000313|Proteomes:UP000076574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vaf07 {ECO:0000313|EMBL:KZD20600.1,
RC   ECO:0000313|Proteomes:UP000076574};
RA   Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT   "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT   Fed.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in beta-(1-->2)glucan export. Transmembrane domains
CC       (TMD) form a pore in the inner membrane and the ATP-binding domain
CC       (NBD) is responsible for energy generation.
CC       {ECO:0000256|ARBA:ARBA00024722}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       {ECO:0000256|ARBA:ARBA00005417}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZD20600.1}.
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DR   EMBL; LVYV01000055; KZD20600.1; -; Genomic_DNA.
DR   RefSeq; WP_068738161.1; NZ_LVYV01000055.1.
DR   AlphaFoldDB; A0A163X9E6; -.
DR   STRING; 943830.A4A58_17835; -.
DR   OrthoDB; 9804259at2; -.
DR   Proteomes; UP000076574; Unassembled WGS sequence.
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   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   CDD; cd18552; ABC_6TM_MsbA_like; 1.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KZD20600.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022597}.
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..317
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          351..585
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   600 AA;  65505 MW;  69EC393D879D215D CRC64;
     MAKITRKVTD DPYGAWALIR RLVAEQAVTY WRRYLLAFLL MAVSAATTAG AAYMLGEVIN
     QAYVDKSIER IALFSGFVVV IFLIKGASTY GHTVILSKIS NAIVANNQRR LFAKLMNESI
     GFFSERHSSE FLQRLTAGAN SVTQVLSLLI NAVGRDLLSL IALVGVMVMQ DPYMALFGFL
     VAPPAMLVLR KLVRRIKGLA RNQFTGTTEI LEVMQESLQG IRTVKAFTLE QTMQQRMEAS
     ITAVEQNANR MARVSSRSSP LMETLGGFAI AASLMYGGYR VVAMGATPGQ FFSFVTAFLL
     AYEPAKRLAR LNIDLNSQII GAHTLLEIVD SPASEPNDDH KPALKLTDAR VELQDVTFRY
     RPNEVVLNRM SFVAEPGKVT ALVGPSGGGK STVLALLLRL YEVSEGDITI DGQSIGQVSR
     RSLRGQTAYV GQDVYLFRGT IRENIAFGKP GATEDEIVAA AKAASAHDFI LGFPLGYETP
     VGEHGAQLSG GQRQRIAIAR ALVKNAPIIL LDEATAALDS ESEKSVQEAI EHLCQNRTTI
     VIAHRLHTIM HADAILVVEG GEIVERGRHD DLLRRGGRYA SFFRLQHRDA SPLAPLDASA
//
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