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Database: UniProt
Entry: A0A257KSN0_9BRAD
LinkDB: A0A257KSN0_9BRAD
Original site: A0A257KSN0_9BRAD 
ID   A0A257KSN0_9BRAD        Unreviewed;       592 AA.
AC   A0A257KSN0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Type I secretion system permease/ATPase {ECO:0000313|EMBL:OYU90169.1};
GN   ORFNames=CFE29_14335 {ECO:0000313|EMBL:OYU90169.1};
OS   Bradyrhizobiaceae bacterium PARB1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=2015576 {ECO:0000313|EMBL:OYU90169.1, ECO:0000313|Proteomes:UP000216768};
RN   [1] {ECO:0000313|EMBL:OYU90169.1, ECO:0000313|Proteomes:UP000216768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PARB1 {ECO:0000313|EMBL:OYU90169.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU90169.1}.
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DR   EMBL; NKIY01000003; OYU90169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257KSN0; -.
DR   Proteomes; UP000216768; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
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   GO; GO:0030253; P:protein secretion by the type I secretion system; 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; IPR010128; ATPase_T1SS_PrtD-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR01842; type_I_sec_PrtD; 1.
DR   PANTHER; PTHR24221:SF248; ABC TRANSPORTER TRANSMEMBRANE REGION-RELATED; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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        29..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..308
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          339..575
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   592 AA;  62739 MW;  FDDF37A54E40CAD9 CRC64;
     MTAVPSTGRA DAAATHDVPI AALASCRSAL LSVGIFSAVV NVLMLTGSIY MLQVYDRVIP
     SRSVPTLVSL SIIVIAIYAV QGVFDWLRQR ILSRIGAALD QALWEPVNSA ILRSPLKSNR
     SNGVQLAHDL DSVRGFLSGL GPTTLFDLPW MPLYLAGCFL LHPYLGWTLV AGAVILFGIA
     LLAEILTRKP TREASRNAAA RNVQLEAARR NAEVIAALGM ERRFVNRIGI ANSDQIAAQQ
     RGADISASLG TLSKTLRFLL QSTLLGIGAW LVIEGHATSG VMIASSIMGS RALAPVELAI
     SVWRPFIAAR QAWQRLRTAL APESENVAAV APDRARRVLT VDQVFVMAPG GNKAIVQNAT
     FKLEAGHAVG IIGPSASGKS SLTRALVGIW PAARGDIRLD GATLDQWPAE SRGDMIGYLP
     QAVELFDGTV AENIARFDPQ LDSNAVIAAA KAAGAYDMIL GLPKGFEMQV GEAGSALSGG
     QRQRVALARA LYKDPFMVVL DEPNANLDGE GDAALARAVK GVRARGGIAI IVAHRPAALA
     SVDLVMTFAN GQIQAFGPKD EILRKALASQ NPPSNVVTQP VHDMRMTADS RS
//
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