(data stored in SCRATCH zone)

HOGENOM: FRAP2_2_PE1011

ID   FRAP2_2_PE1011                       STANDARD;      PRT;   609 AA.
AC   FRAP2_2_PE1011; B0TWX7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Lipid A transport protein, ABC type transporter,
DE   ATP-binding and permease protein; (FRAP2_2.PE1011).
GN   OrderedLocusNames=Fphi_1011;
OS   FRANCISELLA PHILOMIRAGIA SUBSP. PHILOMIRAGIA ATCC 25017.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=484022;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FRAP2_2.PE1011.
CC       Francisella philomiragia subsp. philomiragia ATCC 25017, complete genom
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:B0TWX7_FRAP2
CC   -!- FUNCTION: Involved in lipid A export and possibly also in
CC       glycerophospholipid export and for biogenesis of the outer
CC       membrane. Transmembrane domains (TMD) form a pore in the inner
CC       membrane and the ATP-binding domain (NBD) is responsible for
CC       energy generation (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC   -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
CC   -!- SIMILARITY: Contains 1 ABC transporter domain.
CC   -!- GENE_FAMILY: HOG10000000 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0TWX7; -.
DR   EMBL; CP000937; ABZ87235.1; -; Genomic_DNA.
DR   RefSeq; YP_001677736.1; NC_010336.1.
DR   ProteinModelPortal; B0TWX7; -.
DR   STRING; B0TWX7; -.
DR   GeneID; 5907141; -.
DR   GenomeReviews; CP000937_GR; Fphi_1011.
DR   KEGG; fph:Fphi_1011; -.
DR   OMA; THIASEV; -.
DR   ProtClustDB; CLSK934370; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017940; ABC_transporter_type1.
DR   InterPro; IPR011917; ABC_transpr_lipidA.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC_TM_1; 1.
DR   TIGRFAMs; TIGR02203; MsbA_lipidA; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51239; MSBA; 1.
DR   HOGENOMDNA; FRAP2_2.PE1011; -.
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Hydrolase; Lipid transport; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   609 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MANLIDKIDL KSQSSGNLSG EMVNKEKVGT LYKRLLLQVK HLWYFLVIAA IGSVFFSAAD
     ASMIYLINPI LNYGFGPGGD ITKQSASILM LMGVGMVGLL ALRSVGSFLS QYFIGSLGQK
     VVYKFRKDIY KRFMNLPASF FDKHSSGQII SRLLYNVDQV TEATSTAIIT VVQDGTFVIG
     LIIVMVVSSW QLSLFLIIIG PFLGLFISII NKKFRSLSRN TQSSMGNVTH IAEETIRNYK
     EIRIFGAQQK QQNKFFKNLD YTYSQQIRTI ALDALTSPVI QIIASLVLAF SLFTIAIFGT
     NEGGSSSWLT AGSFASFFAA AAAILKPIKN LTKVNVVIQK AVAATEDIFY ILDYPSEKET
     GKKEIEKVSG KVTIKDVSFA FADHKVLNGV STEIEAGETV AFVGKSGSGK TTLTSIISRF
     YTQQQGQILL DNIDIRDLTL ENLRSHLSMV SQNVHLFDDT VFNNIAFGLS RDVSEEEVVD
     ALKRANAYEF VQELSDGIRT NIGNNGSKLS GGQRQRLSIA RALLKNAPVL IFDEATSALD
     NESERVVQQA LESLTKSCTT IVIAHRLSTV ENADKIVVMD DGKIVESGKH EELLAKGGLY
     TRLYQSGLQ
//

If you have problems or comments...

PBIL Back to PBIL home page