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LPTB_SHIFL
ID   LPTB_SHIFL              Reviewed;         241 AA.
AC   P0A9V4; P31220;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Lipopolysaccharide export system ATP-binding protein LptB;
DE            EC=7.5.2.-;
GN   Name=lptB; OrderedLocusNames=SF3241, S3459;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex LptBFG involved in the
CC       translocation of lipopolysaccharide (LPS) from the inner membrane to
CC       the outer membrane. Probably responsible for energy coupling to the
CC       transport system (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. The LptBFG transporter is composed of two ATP-binding proteins
CC       (LptB) and two transmembrane proteins (LptF and LptG) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Outer membrane
CC       lipopolysaccharide export (TC 1.B.42) family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN44707.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18521.1; -; Genomic_DNA.
DR   RefSeq; NP_709000.1; NC_004337.2.
DR   RefSeq; WP_000224099.1; NZ_WPGW01000004.1.
DR   PDB; 6S8G; EM; 3.50 A; A/B=1-241.
DR   PDB; 6S8H; EM; 3.70 A; A/B=1-241.
DR   PDB; 6S8N; EM; 3.10 A; A/B=1-241.
DR   PDBsum; 6S8G; -.
DR   PDBsum; 6S8H; -.
DR   PDBsum; 6S8N; -.
DR   AlphaFoldDB; P0A9V4; -.
DR   SMR; P0A9V4; -.
DR   STRING; 198214.SF3241; -.
DR   PRIDE; P0A9V4; -.
DR   EnsemblBacteria; AAN44707; AAN44707; SF3241.
DR   EnsemblBacteria; AAP18521; AAP18521; S3459.
DR   GeneID; 1027080; -.
DR   GeneID; 67415965; -.
DR   KEGG; sfl:SF3241; -.
DR   KEGG; sfx:S3459; -.
DR   PATRIC; fig|198214.7.peg.3842; -.
DR   HOGENOM; CLU_000604_1_2_6; -.
DR   OMA; LPMYQRA; -.
DR   OrthoDB; 1220708at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd03218; ABC_YhbG; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR032823; BCA_ABC_TP_C.
DR   InterPro; IPR030921; LPS_export_LptB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF12399; BCA_ABC_TP_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR04406; LPS_export_lptB; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm;
KW   Membrane; Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..241
FT                   /note="Lipopolysaccharide export system ATP-binding protein
FT                   LptB"
FT                   /id="PRO_0000093181"
FT   DOMAIN          4..237
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          8..22
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:6S8G"
FT   HELIX           44..50
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:6S8G"
FT   HELIX           72..75
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   TURN            76..79
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:6S8G"
FT   HELIX           95..103
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   HELIX           118..124
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:6S8G"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   HELIX           146..152
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          157..167
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   HELIX           173..185
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   STRAND          214..217
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   HELIX           221..224
FT                   /evidence="ECO:0007829|PDB:6S8N"
FT   HELIX           230..233
FT                   /evidence="ECO:0007829|PDB:6S8N"
SQ   SEQUENCE   241 AA;  26801 MW;  6041495BDDCDFA72 CRC64;
     MATLTAKNLA KAYKGRRVVE DVSLTVNSGE IVGLLGPNGA GKTTTFYMVV GIVPRDAGNI
     IIDDDDISLL PLHARARRGI GYLPQEASIF RRLSVYDNLM AVLQIRDDLS AEQREDRANE
     LMEEFHIEHL RDSMGQSLSG GERRRVEIAR ALAANPKFIL LDEPFAGVDP ISVIDIKRII
     EHLRDSGLGV LITDHNVRET LAVCERAYIV SQGHLIAHGT PTEILQDEHV KRVYLGEDFR
     L
 
 
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