CYCX_NITEU
ID CYCX_NITEU Reviewed; 233 AA.
AC Q50926;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable tetraheme cytochrome c-type;
DE Flags: Precursor;
GN Name=cycX1; OrderedLocusNames=NE2336;
GN and
GN Name=cycX2; OrderedLocusNames=NE0959;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=8195067; DOI=10.1128/jb.176.11.3148-3153.1994;
RA Bergmann D.J., Arciero D.M., Hooper A.B.;
RT "Organization of the hao gene cluster of Nitrosomonas europaea: genes for
RT two tetraheme c cytochromes.";
RL J. Bacteriol. 176:3148-3153(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family. {ECO:0000305}.
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DR EMBL; U08288; AAA19968.1; -; Unassigned_DNA.
DR EMBL; AL954747; CAD84870.1; -; Genomic_DNA.
DR EMBL; AL954747; CAD86248.1; -; Genomic_DNA.
DR PIR; B59037; B59037.
DR RefSeq; WP_011111568.1; NC_004757.1.
DR AlphaFoldDB; Q50926; -.
DR STRING; 228410.NE0959; -.
DR EnsemblBacteria; CAD84870; CAD84870; NE0959.
DR EnsemblBacteria; CAD86248; CAD86248; NE2336.
DR KEGG; neu:NE0959; -.
DR KEGG; neu:NE2336; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_096753_2_0_4; -.
DR OMA; HIGMDTI; -.
DR OrthoDB; 1683334at2; -.
DR PhylomeDB; Q50926; -.
DR BioCyc; MetaCyc:MON-17538; -.
DR Proteomes; UP000001416; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3820.10; -; 1.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR InterPro; IPR038266; NapC/NirT_cytc_sf.
DR Pfam; PF03264; Cytochrom_NNT; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..233
FT /note="Probable tetraheme cytochrome c-type"
FT /id="PRO_0000006592"
FT REGION 182..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 42
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 45
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|UniProtKB:Q72EF4"
FT BINDING 67
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 70
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 71
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|UniProtKB:Q72EF4"
FT BINDING 93
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|UniProtKB:Q72EF4"
FT BINDING 131
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 134
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 135
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|UniProtKB:Q72EF4"
FT BINDING 159
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 162
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 163
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|UniProtKB:Q72EF4"
FT BINDING 168
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|UniProtKB:Q72EF4"
FT SITE 165
FT /note="Interaction with NrfA"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
SQ SEQUENCE 233 AA; 25486 MW; A0F898F69F65DEC3 CRC64;
MTRLQKGSIG TLLTGALLGI VLVAVVFGGE AALSTEEFCT SCHSMTYPQA ELKQSTHYGA
LGVNPGCKDC HIPQGIENFH LAVATHAIDG ARELYLELVN DYSTLEKFNE RRLEMAHDAR
MNLKKWDSIT CRTCHKKPAP PGESAQAEHK KMETEGATCI DCHQNLVHEE VPMTDLNASI
AQGKLVLKPE DDGDDEEADE DEDEETEEAD DSSDSESASS SDNSDNEDDN NDE
