ID F7XUB7_MIDMI Unreviewed; 818 AA.
AC F7XUB7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative ABC transporter ATP-binding protein {ECO:0000313|EMBL:AEI89476.1};
GN OrderedLocusNames=midi_01200 {ECO:0000313|EMBL:AEI89476.1};
OS Midichloria mitochondrii (strain IricVA).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Midichloriaceae; Midichloria.
OX NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI89476.1, ECO:0000313|Proteomes:UP000006639};
RN [1] {ECO:0000313|EMBL:AEI89476.1, ECO:0000313|Proteomes:UP000006639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IricVA {ECO:0000313|EMBL:AEI89476.1,
RC ECO:0000313|Proteomes:UP000006639};
RX PubMed=21690562; DOI=10.1093/molbev/msr159;
RA Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
RA Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
RA Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
RT "Phylogenomic evidence for the presence of a flagellum and cbb3 oxidase in
RT the free-living mitochondrial ancestor.";
RL Mol. Biol. Evol. 28:3285-3296(2011).
CC -!- FUNCTION: Part of an ABC transporter complex. 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:ARBA00024725}.
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}.
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DR EMBL; CP002130; AEI89476.1; -; Genomic_DNA.
DR AlphaFoldDB; F7XUB7; -.
DR STRING; 696127.midi_01200; -.
DR KEGG; mmn:midi_01200; -.
DR HOGENOM; CLU_345404_0_0_5; -.
DR Proteomes; UP000006639; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR NCBIfam; TIGR00128; fabD; 1.
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 Pfam; PF00698; Acyl_transf_1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 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:AEI89476.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006639};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..206
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 251..485
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 818 AA; 90025 MW; D0C6A3036C9696F9 CRC64;
MPKFEANIRT SMFNYVSNHS HSYFVQTHVG GIAQRISDMP KSAKLVIDDL LTVFIPLIVS
IIASSSVFLS MHPLLAAIFF TWLGLHFTLC VFFCLKAANS VSVQSAARAL LQGKIVDSMT
NHLSVKLFTA HQHEMQTIKE AQADELQKYR YSLIYIEKFK MLLSLISIIN ITLLLYLAIK
LWQQGQITIG DIVFTINSTL GLMTNLWFTG DEISYMFYEI GVCKQSLILL EEPTEISEST
LKQIKVTQGK IEFDNVSFNY HNNGNIFKNK SLVIHGGQKV GLVGFSGSGK TTFANLIMRL
YEVSSGTVKI DDQDVSQASL LSLRSNIAFI PQDPFLFHRS VLENIRYGNI NATDEEVKEV
AKKAECDSFI MNLEHGYDTI VGERGSKLSG GQRQRIAIAR AMLKNAPIVI MDEATSALDS
VTERLIEKSL QHLMVNKTAI VIAHRLSTLL HLDRILVFEK GNIVGDGTHE ELLTKGGRYA
MLWHMQQSGL LPEHDNGKKG IKMDKNKSSL LFPGQGSQVV GMGVELFNTF NEAKEVFSLI
DETLKQNLSQ LMFSGELEEL TLTANAQPAI MAVSLAVMAV LEKQLNLTIQ DLCNVAAGHS
LGEYSALAAS GVFSLTDTAS LLRVRGDAMQ SAVNPGEGAM VALIGTDLDS AQKLCNHVAN
YGACQIANDN GAGQIVLSGA TIAIDKAIES ATNFGVKKAI KLKVSAPFHS SLMQSAAFKM
EQALKGVAIH NPTIDVMANF NVEKHHESIT KDLLVSQVAG SVRWRETMEK ITTHYEVDTF
IEIGPGQVLS GIAKRMYPGS NVFNLHTPKN IEEFSDFL
//
