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
//