NAPB_HAEIN
ID NAPB_HAEIN Reviewed; 150 AA.
AC P44654;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB;
DE Flags: Precursor;
GN Name=napB; OrderedLocusNames=HI_0347;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP PROTEIN SEQUENCE OF 27-31, FUNCTION, ABSORPTION SPECTROSCOPY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PTM, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=11389694; DOI=10.1042/0264-6021:3560851;
RA Brige A., Cole J.A., Hagen W.R., Guisez Y., Van Beeumen J.J.;
RT "Overproduction, purification and novel redox properties of the dihaem
RT cytochrome c, NapB, from Haemophilus influenzae.";
RL Biochem. J. 356:851-858(2001).
RN [3]
RP CRYSTALLIZATION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=11223519; DOI=10.1107/s0907444900018011;
RA Brige A., Leys D., Van Beeumen J.J.;
RT "Crystallization and preliminary X-ray analysis of the recombinant dihaem
RT cytochrome c (NapB) from Haemophilus influenzae.";
RL Acta Crystallogr. D 57:418-420(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 28-150 IN COMPLEX WITH HEME C,
RP AND PTM.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=11939777; DOI=10.1021/bi012144b;
RA Brige A., Leys D., Meyer T.E., Cusanovich M.A., Van Beeumen J.J.;
RT "The 1.25 A resolution structure of the diheme NapB subunit of soluble
RT nitrate reductase reveals a novel cytochrome c fold with a stacked heme
RT arrangement.";
RL Biochemistry 41:4827-4836(2002).
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. {ECO:0000269|PubMed:11389694}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are -25 mV and -175 mV. {ECO:0000269|PubMed:11389694};
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11223519,
CC ECO:0000269|PubMed:11389694}.
CC -!- PTM: Binds 2 heme C groups per subunit.
CC -!- MASS SPECTROMETRY: Mass=14748.68; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11223519};
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000305}.
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DR EMBL; L42023; AAC22008.1; -; Genomic_DNA.
DR PIR; C64149; C64149.
DR RefSeq; NP_438511.1; NC_000907.1.
DR PDB; 1JNI; X-ray; 1.25 A; A=28-150.
DR PDBsum; 1JNI; -.
DR AlphaFoldDB; P44654; -.
DR SMR; P44654; -.
DR STRING; 71421.HI_0347; -.
DR EnsemblBacteria; AAC22008; AAC22008; HI_0347.
DR KEGG; hin:HI_0347; -.
DR PATRIC; fig|71421.8.peg.366; -.
DR eggNOG; COG3043; Bacteria.
DR HOGENOM; CLU_103367_3_0_6; -.
DR OMA; PIVPNEF; -.
DR PhylomeDB; P44654; -.
DR BioCyc; HINF71421:G1GJ1-363-MON; -.
DR EvolutionaryTrace; P44654; -.
DR Proteomes; UP000000579; 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; IBA:GO_Central.
DR DisProt; DP00899; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:11389694"
FT CHAIN 27..150
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_0000006589"
FT BINDING 70
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 BINDING 84
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11939777"
FT BINDING 87
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11939777"
FT BINDING 88
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 BINDING 105
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 BINDING 124
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11939777"
FT BINDING 127
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11939777"
FT BINDING 128
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 HELIX 85..88
FT /evidence="ECO:0007829|PDB:1JNI"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1JNI"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1JNI"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1JNI"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1JNI"
SQ SEQUENCE 150 AA; 16255 MW; C5E98C4E1B29E01F CRC64;
MINMTKQVSK ILAGLFTALF AGSLMASDAP AVGKDLTQAA ENIPPAFHNA PRQGELPALN
YVNQPPMVPH SVANYQVTKN VNQCLNCHSP ENSRLSGATR ISPTHFMDRD GKVGSSSSPR
RYFCLQCHVS QANVDPIVPN DFKPMKGYGN
