ID Q7VYU2_BORPE Unreviewed; 261 AA.
AC Q7VYU2;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Transport permease protein {ECO:0000256|RuleBase:RU361157};
GN Name=nodJ {ECO:0000313|EMBL:CAE41511.1};
GN OrderedLocusNames=BP1215 {ECO:0000313|EMBL:CAE41511.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41511.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- FUNCTION: Part of the ABC transporter complex NodIJ involved in the
CC export of the nodulation factors (Nod factors), the bacterial signal
CC molecules that induce symbiosis and subsequent nodulation induction.
CC Nod factors are LCO (lipo-chitin oligosaccharide), a modified beta-1,4-
CC linked N-acetylglucosamine oligosaccharide. This subunit encodes the
CC transporter. {ECO:0000256|ARBA:ARBA00025119}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (NodI) and
CC two transmembrane proteins (NodJ). {ECO:0000256|ARBA:ARBA00011350}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|RuleBase:RU361157}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|RuleBase:RU361157}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC Lipooligosaccharide exporter (TC 3.A.1.102) subfamily.
CC {ECO:0000256|ARBA:ARBA00008394}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361157}.
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; BX640414; CAE41511.1; -; Genomic_DNA.
DR RefSeq; NP_879988.1; NC_002929.2.
DR RefSeq; WP_003818606.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VYU2; -.
DR STRING; 257313.BP1215; -.
DR PaxDb; 257313-BP1215; -.
DR GeneID; 69601129; -.
DR KEGG; bpe:BP1215; -.
DR PATRIC; fig|257313.5.peg.1309; -.
DR eggNOG; COG0842; Bacteria.
DR HOGENOM; CLU_039483_3_1_4; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0015772; P:oligosaccharide transport; IEA:InterPro.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR047817; ABC2_TM_bact-type.
DR InterPro; IPR000412; ABC_2_transport.
DR InterPro; IPR005981; ABC_transptNodJ.
DR NCBIfam; TIGR01291; nodJ; 1.
DR PANTHER; PTHR43229; NODULATION PROTEIN J; 1.
DR PANTHER; PTHR43229:SF2; NODULATION PROTEIN J; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR PIRSF; PIRSF006648; DrrB; 1.
DR PRINTS; PR00164; ABC2TRNSPORT.
DR PROSITE; PS51012; ABC_TM2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|RuleBase:RU361157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361157};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000002676};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361157};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361157}; Transport {ECO:0000256|RuleBase:RU361157}.
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 64..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 233..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT DOMAIN 32..258
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000259|PROSITE:PS51012"
SQ SEQUENCE 261 AA; 28067 MW; 75CCBB3BC1CEE144 CRC64;
MSAGAWGWPP LTRRCVAVLR RNFLVWRKTA LTTVLGDVLD PVVALLALGF GLGALLPGIE
GVPYVTFLSA GSMCVGALYG ATFEATYNAF SRLHVQRTWD AMLSTPLDLD DVVWAEILWA
AAKALKSGIA ILLVVVALDI ARAPTLLWVP PVLALAGLAF ASMALVVSAL ARGYEFFMYY
FTLGVTPMVF LSGVFFPASQ LPAALAGPLQ WLPVAPAVNL IRPLTLGQVP HAWWADVAQL
AVTAALGIWL VAVLMRRRLL R
//
