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LSRA_PHOLU
ID   LSRA_PHOLU              Reviewed;         511 AA.
AC   Q2PBM0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Autoinducer 2 import ATP-binding protein LsrA {ECO:0000250|UniProtKB:P77257};
DE            Short=AI-2 import ATP-binding protein LsrA {ECO:0000250|UniProtKB:P77257};
DE            EC=7.6.2.13 {ECO:0000250|UniProtKB:P77257};
GN   Name=lsrA;
OS   Photorhabdus luminescens (Xenorhabdus luminescens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=29488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29999 / DSM 3368 / BCRC 14801 / CIP 106429 / NCIMB 12670 / Hb;
RX   PubMed=16385072; DOI=10.1128/jb.188.2.809-814.2006;
RA   Gaudriault S., Duchaud E., Lanois A., Canoy A.-S., Bourot S., DeRose R.,
RA   Kunst F., Boemare N., Givaudan A.;
RT   "Whole-genome comparison between Photorhabdus strains to identify genomic
RT   regions involved in the specificity of nematode interaction.";
RL   J. Bacteriol. 188:809-814(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex LsrABCD involved in
CC       autoinducer 2 (AI-2) import. Responsible for energy coupling to the
CC       transport system. {ECO:0000250|UniProtKB:P77257}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + (2R,4S)-2-methyl-2,3,3,4-
CC         tetrahydroxytetrahydrofuran-[AI-2-binding protein]Side 1 = ADP +
CC         phosphate + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuranSide
CC         2 + [AI-2-binding protein]Side 1.; EC=7.6.2.13;
CC         Evidence={ECO:0000250|UniProtKB:P77257};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (LsrA),
CC       two transmembrane proteins (LsrC and LsrD) and a solute-binding protein
CC       (LsrB). {ECO:0000250|UniProtKB:P77257}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P77257}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P77257}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. AI-2
CC       autoinducer porter (TC 3.A.1.2.8) family. {ECO:0000305}.
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DR   EMBL; AJ967010; CAI91190.1; -; Genomic_DNA.
DR   RefSeq; WP_049584345.1; NZ_FMWJ01000024.1.
DR   AlphaFoldDB; Q2PBM0; -.
DR   SMR; Q2PBM0; -.
DR   STRING; 29488.KS18_20635; -.
DR   GeneID; 45657233; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
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-coupled transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1905887; P:autoinducer AI-2 transmembrane transport; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR030281; LsrA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43790:SF2; PTHR43790:SF2; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Repeat; Translocase; Transport.
FT   CHAIN           1..511
FT                   /note="Autoinducer 2 import ATP-binding protein LsrA"
FT                   /id="PRO_0000351297"
FT   DOMAIN          12..240
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          263..503
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   511 AA;  56019 MW;  5A334E21326207B6 CRC64;
     MLHNNTAVPP LLEVSGISKQ FSGVMVLKHI DFTLLPGQIH ALLGGNGAGK STLMKIIAGI
     EQPDKGILKI SGHHVSHLNP TKAHQLGIYL IPQEPLLFPN LSVQENILFR LPKHQVDKSK
     MKQLLALLGC QLDLHVSASS LNVADQQLVE IMRGLMRNSK ILILDEPTAS LTPAETERLF
     TQLRELQQQG VGIIFISHKI PEIYQLAGQV SVMRDGSIAL SGEIRDYTTD EIIQAITPVA
     KNQPLNGTQK LGLDLSNSPS QTASDRPILT VTKLSGEGFC NITFSVKPGE ILGLAGVVGA
     GRTELAETLY GLRPAISGEI KLKQHSVNGL KTAQRLAQGL VYLPEDRQSS GLFLDSSLGW
     NICSLTHNRN TFWIRPAYDT AVLERYCQTL NIKFSHINQP IKTLSGGNQQ KILIAKCLEA
     HPAVLIIDEP TRGVDVAARN DIYQLIRHIA QQQVAIIFIS SDLDEVVRMA DRVLVMHQGE
     INGELTKQQM DVDTIMHIAF GEHKPQQAAS C
 
 
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