ID K9UY59_9CYAN Unreviewed; 605 AA.
AC K9UY59;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Xenobiotic-transporting ATPase {ECO:0000313|EMBL:AFY99919.1};
DE EC=3.6.3.44 {ECO:0000313|EMBL:AFY99919.1};
GN ORFNames=Cal6303_0854 {ECO:0000313|EMBL:AFY99919.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFY99919.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFY99919.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFY99919.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003610; AFY99919.1; -; Genomic_DNA.
DR RefSeq; WP_015196574.1; NC_019751.1.
DR AlphaFoldDB; K9UY59; -.
DR STRING; 1170562.Cal6303_0854; -.
DR KEGG; calt:Cal6303_0854; -.
DR PATRIC; fig|1170562.3.peg.929; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_3; -.
DR OrthoDB; 9762790at2; -.
DR Proteomes; UP000010477; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR43394:SF1; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:AFY99919.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..324
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 359..599
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 605 AA; 68536 MW; 8D76B81E6CAD7D6B CRC64;
MPTIQKLQHK LKQALRLLPA LRLVWQAAPG WTIVYIVLII VQGTLPLLLL YLTKLVIDTV
VNSLTIADKV SSGKQLIILL LLTGLVTFVS TICNSFAELV NTAQSQRVTD YMSSIIHAKS
IEVDLDYYEN SQYHDALKRA QEEASYRPNR ILNNLVAVTQ NSISLVAMLG LMLSLHWGIA
SVLFMAAFPS VLVRVKFADI MYRWHRKRTT MERESHYLSW LLTGDIFAKE IRLFDLGILF
SQRFDNLRQK LFQENIAISR KRSVATFVAQ TIATILMLAA YGFIIYQAFL GVIRIGDLVL
YHEGLKRGQD SLTGVLGRLS SLYEDNLFLA NLYEFLDIKP QITQPNHPQA FPQPMRTGIV
FDNVNFQYST TTRQALKNIN LTIKPGEVIA LVGENGSGKT TLIKLLCRLY DPTSGNITID
GIDINNFDIT ELRRQFSVIF QDYVKYHFTA QENIWLGNVD ISPIDDKVTI AARRSGADTV
IQSLPQGYDT MLGKWFDQGE ELSIGQWQKV ALARAFLRNS QVIVLDEPTS AMDPKAEAEV
FEGFRQLIKN QAAILISHRL STVKMADRIY VMDKGRIVES GNHEKLMQMG GSYAYLFETQ
AKNYR
//
