NAPB_SHIFL
ID NAPB_SHIFL Reviewed; 149 AA.
AC P0ABL4; P33933; P76453;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB;
DE Flags: Precursor;
GN Name=napB; OrderedLocusNames=SF2287, S2417;
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: Electron transfer subunit of the periplasmic nitrate
CC reductase complex NapAB. Receives electrons from the membrane-anchored
CC tetraheme c-type NapC protein and transfers these to NapA subunit, thus
CC allowing electron flow between membrane and periplasm. Essential for
CC periplasmic nitrate reduction with nitrate as the terminal electron
CC acceptor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Binds 2 heme C groups per subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000305}.
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DR EMBL; AE005674; AAN43806.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP17623.1; -; Genomic_DNA.
DR RefSeq; NP_708099.2; NC_004337.2.
DR RefSeq; WP_000835174.1; NZ_WPGW01000022.1.
DR AlphaFoldDB; P0ABL4; -.
DR SMR; P0ABL4; -.
DR STRING; 198214.SF2287; -.
DR EnsemblBacteria; AAN43806; AAN43806; SF2287.
DR EnsemblBacteria; AAP17623; AAP17623; S2417.
DR GeneID; 1025488; -.
DR GeneID; 60669099; -.
DR KEGG; sfl:SF2287; -.
DR KEGG; sfx:S2417; -.
DR PATRIC; fig|198214.7.peg.2738; -.
DR HOGENOM; CLU_103367_3_0_6; -.
DR OMA; PIVPNEF; -.
DR OrthoDB; 1650975at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR005591; NapB.
DR PANTHER; PTHR38604; PTHR38604; 1.
DR Pfam; PF03892; NapB; 1.
DR PIRSF; PIRSF006105; NapB; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..149
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_0000042811"
FT BINDING 69
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 104
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 123
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 149 AA; 16297 MW; 6F38F13C092178AF CRC64;
MKSHDLKKAL CQWTAMLALV VSGAVWAANG VDFSQSPEVS GTQEGAIRMP KEQDRMPLNY
VNQPPMIPHS VEGYQVTTNT NRCLQCHGVE SYRTTGAPRI SPTHFMDSDG KVGAEVAPRR
YFCLQCHVPQ ADTAPIVGNT FTPSKGYGK
