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Database: UniProt
Entry: NRFB_ECOLI
LinkDB: NRFB_ECOLI
Original site: NRFB_ECOLI 
ID   NRFB_ECOLI              Reviewed;         188 AA.
AC   P0ABL1; P32707; P76790; Q2M6N3;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-OCT-2017, entry version 92.
DE   RecName: Full=Cytochrome c-type protein NrfB;
DE   Flags: Precursor;
GN   Name=nrfB; Synonyms=yjcI; OrderedLocusNames=b4071, JW4032;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8057835; DOI=10.1111/j.1365-2958.1994.tb01004.x;
RA   Hussain H.A., Grove J., Griffiths L., Busby S., Cole J.;
RT   "A seven-gene operon essential for formate-dependent nitrite reduction
RT   to ammonia by enteric bacteria.";
RL   Mol. Microbiol. 12:153-163(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
RA   Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT   region from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   CHARACTERIZATION AS A CYTOCHROME C.
RX   PubMed=8039676; DOI=10.1111/j.1574-6968.1994.tb06872.x;
RA   Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H.,
RA   Pommier J., Mejean V., Cole J.A.;
RT   "A reassessment of the range of c-type cytochromes synthesized by
RT   Escherichia coli K-12.";
RL   FEMS Microbiol. Lett. 119:89-94(1994).
CC   -!- FUNCTION: Plays a role in nitrite reduction.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- PTM: Binds 5 heme groups per subunit. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC43165.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; X72298; CAA51042.1; -; Genomic_DNA.
DR   EMBL; U00006; AAC43165.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77041.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78073.1; -; Genomic_DNA.
DR   RefSeq; NP_418495.2; NC_000913.3.
DR   RefSeq; WP_001295391.1; NZ_LN832404.1.
DR   PDB; 2OZY; X-ray; 1.74 A; A=26-188.
DR   PDB; 2P0B; X-ray; 1.74 A; A=26-188.
DR   PDBsum; 2OZY; -.
DR   PDBsum; 2P0B; -.
DR   ProteinModelPortal; P0ABL1; -.
DR   SMR; P0ABL1; -.
DR   BioGrid; 4259404; 7.
DR   IntAct; P0ABL1; 3.
DR   STRING; 316407.85676823; -.
DR   PaxDb; P0ABL1; -.
DR   PRIDE; P0ABL1; -.
DR   EnsemblBacteria; AAC77041; AAC77041; b4071.
DR   EnsemblBacteria; BAE78073; BAE78073; BAE78073.
DR   GeneID; 948573; -.
DR   KEGG; ecj:JW4032; -.
DR   KEGG; eco:b4071; -.
DR   PATRIC; fig|1411691.4.peg.2633; -.
DR   EchoBASE; EB1888; -.
DR   EcoGene; EG11945; nrfB.
DR   eggNOG; ENOG4105JJ8; Bacteria.
DR   eggNOG; ENOG411128Q; LUCA.
DR   HOGENOM; HOG000278525; -.
DR   InParanoid; P0ABL1; -.
DR   KO; K04013; -.
DR   PhylomeDB; P0ABL1; -.
DR   BioCyc; EcoCyc:CYTOCHROMEC-MONOMER; -.
DR   BioCyc; MetaCyc:CYTOCHROMEC-MONOMER; -.
DR   UniPathway; UPA00045; -.
DR   EvolutionaryTrace; P0ABL1; -.
DR   PRO; PR:P0ABL1; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0009055; F:electron carrier activity; IDA:EcoCyc.
DR   GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IMP:EcoCyc.
DR   GO; GO:0019645; P:anaerobic electron transport chain; IDA:EcoCyc.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR023155; Cyt_c-552/4.
DR   InterPro; IPR017564; Cyt_c_NO2Rdtase_pentahaem-su.
DR   InterPro; IPR011031; Multihaem_cyt.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   InterPro; IPR010177; Paired_CXXCH_1.
DR   Pfam; PF13435; Cytochrome_C554; 1.
DR   Pfam; PF09699; Paired_CXXCH_1; 1.
DR   SUPFAM; SSF48695; SSF48695; 1.
DR   TIGRFAMs; TIGR03146; cyt_nit_nrfB; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Electron transport; Heme; Iron;
KW   Metal-binding; Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL        1     32       {ECO:0000255}.
FT   CHAIN        33    188       Cytochrome c-type protein NrfB.
FT                                /FTId=PRO_0000006585.
FT   METAL        53     53       Iron (heme 1 axial ligand).
FT                                {ECO:0000250}.
FT   METAL        82     82       Iron (heme 2 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       117    117       Iron (heme 3 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       142    142       Iron (heme 4 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       167    167       Iron (heme 5 axial ligand).
FT                                {ECO:0000250}.
FT   BINDING      49     49       Heme 1 (covalent). {ECO:0000250}.
FT   BINDING      52     52       Heme 1 (covalent). {ECO:0000250}.
FT   BINDING      78     78       Heme 2 (covalent). {ECO:0000250}.
FT   BINDING      81     81       Heme 2 (covalent). {ECO:0000250}.
FT   BINDING     113    113       Heme 3 (covalent). {ECO:0000250}.
FT   BINDING     116    116       Heme 3 (covalent). {ECO:0000250}.
FT   BINDING     138    138       Heme 4 (covalent). {ECO:0000250}.
FT   BINDING     141    141       Heme 4 (covalent). {ECO:0000250}.
FT   BINDING     163    163       Heme 5 (covalent). {ECO:0000250}.
FT   BINDING     166    166       Heme 5 (covalent). {ECO:0000250}.
FT   HELIX        46     49       {ECO:0000244|PDB:2OZY}.
FT   TURN         50     52       {ECO:0000244|PDB:2OZY}.
FT   TURN         55     57       {ECO:0000244|PDB:2OZY}.
FT   HELIX        63     65       {ECO:0000244|PDB:2OZY}.
FT   TURN         70     72       {ECO:0000244|PDB:2OZY}.
FT   STRAND       73     75       {ECO:0000244|PDB:2OZY}.
FT   HELIX        78     82       {ECO:0000244|PDB:2OZY}.
FT   HELIX        89     91       {ECO:0000244|PDB:2OZY}.
FT   STRAND       94     96       {ECO:0000244|PDB:2OZY}.
FT   STRAND       99    101       {ECO:0000244|PDB:2OZY}.
FT   HELIX       106    113       {ECO:0000244|PDB:2OZY}.
FT   TURN        114    116       {ECO:0000244|PDB:2OZY}.
FT   HELIX       119    125       {ECO:0000244|PDB:2OZY}.
FT   HELIX       129    132       {ECO:0000244|PDB:2OZY}.
FT   TURN        133    135       {ECO:0000244|PDB:2OZY}.
FT   HELIX       138    140       {ECO:0000244|PDB:2OZY}.
FT   STRAND      145    148       {ECO:0000244|PDB:2OZY}.
FT   HELIX       150    153       {ECO:0000244|PDB:2OZY}.
FT   HELIX       158    172       {ECO:0000244|PDB:2OZY}.
SQ   SEQUENCE   188 AA;  20714 MW;  33A354F20FAF1548 CRC64;
     MSVLRSLLTA GVLASGLLWS LNGITATPAA QASDDRYEVT QQRNPDAACL DCHKPDTEGM
     HGKHASVINP NNKLPVTCTN CHGQPSPQHR EGVKDVMRFN EPMYKVGEQN SVCMSCHLPE
     QLQKAFWPHD VHVTKVACAS CHSLHPQQDT MQTLSDKGRI KICVDCHSDQ RTNPNFNPAS
     VPLLKEQP
//
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