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 03-AUG-2022, entry version 114.
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 to
RT 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., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT 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., 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 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., Pommier J.,
RA 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=Extended N-terminus.; Evidence={ECO:0000305};
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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_STEB01000014.1.
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 AlphaFoldDB; P0ABL1; -.
DR SMR; P0ABL1; -.
DR BioGRID; 4259404; 17.
DR IntAct; P0ABL1; 3.
DR STRING; 511145.b4071; -.
DR jPOST; P0ABL1; -.
DR PaxDb; P0ABL1; -.
DR PRIDE; P0ABL1; -.
DR EnsemblBacteria; AAC77041; AAC77041; b4071.
DR EnsemblBacteria; BAE78073; BAE78073; BAE78073.
DR GeneID; 66672013; -.
DR GeneID; 948573; -.
DR KEGG; ecj:JW4032; -.
DR KEGG; eco:b4071; -.
DR PATRIC; fig|1411691.4.peg.2633; -.
DR EchoBASE; EB1888; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_104606_2_0_6; -.
DR InParanoid; P0ABL1; -.
DR OMA; NIGPDHR; -.
DR PhylomeDB; P0ABL1; -.
DR BioCyc; EcoCyc:CYTOCHROMEC-MON; -.
DR BioCyc; MetaCyc:CYTOCHROMEC-MON; -.
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 transfer 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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; IPR017564; Cyt_c_NO2Rdtase_pentahaem-su.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR012286; Tetrahaem_cytochrome.
DR Pfam; PF14537; Cytochrom_c3_2; 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; Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..188
FT /note="Cytochrome c-type protein NrfB"
FT /id="PRO_0000006585"
FT BINDING 49
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:2OZY"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2OZY"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2OZY"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2OZY"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2OZY"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2OZY"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:2OZY"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:2OZY"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2OZY"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:2OZY"
FT HELIX 158..172
FT /evidence="ECO:0007829|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
