ARAP_ALKHC
ID ARAP_ALKHC Reviewed; 316 AA.
AC Q9KEF0;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Arabinooligosaccharides transport system permease protein AraP {ECO:0000250|UniProtKB:P94529};
GN Name=araP; OrderedLocusNames=BH0902;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Part of the ABC transporter complex AraNPQ involved in the
CC uptake of arabinooligosaccharides (By similarity). Responsible for the
CC translocation of the substrate across the membrane (By similarity).
CC {ECO:0000250|UniProtKB:P94529}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsmX),
CC two transmembrane proteins (AraP and AraQ) and a solute-binding protein
CC (AraN). {ECO:0000250|UniProtKB:P94529}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. MalFG subfamily. {ECO:0000305}.
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DR EMBL; BA000004; BAB04621.1; -; Genomic_DNA.
DR PIR; F83762; F83762.
DR RefSeq; WP_010897075.1; NC_002570.2.
DR AlphaFoldDB; Q9KEF0; -.
DR SMR; Q9KEF0; -.
DR STRING; 272558.10173517; -.
DR EnsemblBacteria; BAB04621; BAB04621; BAB04621.
DR KEGG; bha:BH0902; -.
DR eggNOG; COG1175; Bacteria.
DR HOGENOM; CLU_016047_0_2_9; -.
DR OMA; CSFPFVM; -.
DR OrthoDB; 1688736at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..316
FT /note="Arabinooligosaccharides transport system permease
FT protein AraP"
FT /id="PRO_0000059953"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 89..304
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 316 AA; 35653 MW; 808DFF8F1EBE6BD6 CRC64;
MLKTGKGTEQ EVVQVHTRKS SRLFTFFNSQ KVVPYVLISP FILSFIVLSF YPTVQAIVMS
FQRVLPSEVT FVGLWNYSRI LNPTFFTALQ NTTTYMILTV VILVSIPMLF AVLLNSKVVK
FRILFRTALF LPALTSVIVA GMVFRLMFSE SDTAVANQIL NWIGLESVEW RYNAWSGMFL
MVVLASWRWM GINILYFLAA LQNVPKELYE AADIDGANVV QKFFYVTLPF LKPVTIFVTT
ISVIGGFRMF EESFVFWEAG SPGNIGLTIV GYLYQEGIQQ NDMGFGAAIG VVLMLIIFVI
SITQLYLTGA FKKGDQ