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NIKB_ECOLI
ID   NIKB_ECOLI              Reviewed;         314 AA.
AC   P33591; Q2M7E0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Nickel transport system permease protein NikB;
GN   Name=nikB; OrderedLocusNames=b3477, JW3442;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7934931; DOI=10.1111/j.1365-2958.1993.tb01247.x;
RA   Navarro C., Wu L.-F., Mandrand-Berthelot M.-A.;
RT   "The nik operon of Escherichia coli encodes a periplasmic binding-protein-
RT   dependent transport system for nickel.";
RL   Mol. Microbiol. 9:1181-1191(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
CC   -!- FUNCTION: Involved in a nickel transport system, probably translocates
CC       nickel through the bacterial inner membrane.
CC   -!- SUBUNIT: Probably forms a heterodimeric pore with NikC.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
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DR   EMBL; X73143; CAA51660.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18452.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76502.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77816.1; -; Genomic_DNA.
DR   PIR; S47696; S47696.
DR   RefSeq; NP_417934.1; NC_000913.3.
DR   RefSeq; WP_000947068.1; NZ_STEB01000004.1.
DR   AlphaFoldDB; P33591; -.
DR   SMR; P33591; -.
DR   BioGRID; 4262492; 20.
DR   ComplexPortal; CPX-4348; Nickel ABC transporter complex.
DR   DIP; DIP-10341N; -.
DR   IntAct; P33591; 1.
DR   STRING; 511145.b3477; -.
DR   TCDB; 3.A.1.5.3; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P33591; -.
DR   PRIDE; P33591; -.
DR   EnsemblBacteria; AAC76502; AAC76502; b3477.
DR   EnsemblBacteria; BAE77816; BAE77816; BAE77816.
DR   GeneID; 66672639; -.
DR   GeneID; 947986; -.
DR   KEGG; ecj:JW3442; -.
DR   KEGG; eco:b3477; -.
DR   PATRIC; fig|1411691.4.peg.3248; -.
DR   EchoBASE; EB2001; -.
DR   eggNOG; COG0601; Bacteria.
DR   HOGENOM; CLU_036879_0_2_6; -.
DR   InParanoid; P33591; -.
DR   OMA; QLPWFTL; -.
DR   PhylomeDB; P33591; -.
DR   BioCyc; EcoCyc:NIKB-MON; -.
DR   BioCyc; MetaCyc:NIKB-MON; -.
DR   PRO; PR:P33591; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0016151; F:nickel cation binding; IDA:EcoCyc.
DR   GO; GO:0015099; F:nickel cation transmembrane transporter activity; IMP:EcoCyc.
DR   GO; GO:0098716; P:nickel cation import across plasma membrane; IC:ComplexPortal.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR045621; BPD_transp_1_N.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR014156; Nickel_NikB.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF19300; BPD_transp_1_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   TIGRFAMs; TIGR02789; nickel_nikB; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Ion transport; Membrane; Nickel;
KW   Nickel transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..314
FT                   /note="Nickel transport system permease protein NikB"
FT                   /id="PRO_0000060120"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        30..103
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        125..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        158..169
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        191..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        253..274
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        296..314
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          98..295
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   CONFLICT        26..27
FT                   /note="ML -> IV (in Ref. 1; CAA51660)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="A -> P (in Ref. 1; CAA51660)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  35248 MW;  B1251307DBE219B3 CRC64;
     MLRYVLRRFL LLIPMVLAAS VIIFLMLRLG TGDPALDYLR LSNLPPTPEM LASTRTMLGL
     DQPLYVQYGT WLWKALHLDF GISFASQRPV LDDMLNFLPA TLELAGAALV LILLTSVPLG
     IWAARHRDRL PDFAVRFIAF LGVSMPNFWL AFLLVMAFSV YLQWLPAMGY GGWQHIILPA
     VSIAFMSLAI NARLLRASML DVAGQRHVTW ARLRGLNDKQ TERRHILRNA SLPMITAVGM
     HIGELIGGTM IIENIFAWPG VGRYAVSAIF NRDYPVIQCF TLMMVVVFVV CNLIVDLLNA
     ALDPRIRRHE GAHA
 
 
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