C554_NITEU
ID C554_NITEU Reviewed; 235 AA.
AC Q57142;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytochrome c-554;
DE AltName: Full=Cytochrome c554;
DE AltName: Full=Hydroxylamine oxidoreductase-linked cytochrome;
DE Flags: Precursor;
GN Name=cycA1; Synonyms=cycA, hcy; OrderedLocusNames=NE2337;
GN and
GN Name=cycA2; Synonyms=cycA; OrderedLocusNames=NE2042;
GN and
GN Name=cycA3; Synonyms=cycA; OrderedLocusNames=NE0960;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=8063110; DOI=10.1016/0378-1119(94)90838-9;
RA Hommes N.G., Sayavedra-Soto L.A., Arp D.J.;
RT "Sequence of hcy, a gene encoding cytochrome c-554 from Nitrosomonas
RT europaea.";
RL Gene 146:87-89(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
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 [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=9808046; DOI=10.1038/2975;
RA Iverson T.M., Arciero D.M., Hsu B.T., Logan M.S.P., Hooper A.B., Rees D.C.;
RT "Heme packing motifs revealed by the crystal structure of the tetraheme
RT cytochrome c554 from Nitrosomonas europaea.";
RL Nat. Struct. Biol. 5:1005-1012(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=11372197; DOI=10.1007/s007750100213;
RA Iverson T.M., Arciero D.M., Hooper A.B., Rees D.C.;
RT "High-resolution structures of the oxidized and reduced states of
RT cytochrome c554 from Nitrosomonas europaea.";
RL J. Biol. Inorg. Chem. 6:390-397(2001).
CC -!- FUNCTION: Involved in ammonia oxidation; accepts electrons directly
CC from hydroxylamine oxidoreductase (HAO).
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 4 heme groups per subunit.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U05951; AAA60464.1; -; Genomic_DNA.
DR EMBL; U08288; AAA19967.1; -; Unassigned_DNA.
DR EMBL; AL954747; CAD84871.1; -; Genomic_DNA.
DR EMBL; AL954747; CAD85953.1; -; Genomic_DNA.
DR EMBL; AL954747; CAD86249.1; -; Genomic_DNA.
DR PIR; A59036; A59036.
DR RefSeq; WP_011111569.1; NC_004757.1.
DR PDB; 1BVB; X-ray; 2.60 A; A=25-235.
DR PDB; 1FT5; X-ray; 1.60 A; A=25-235.
DR PDB; 1FT6; X-ray; 1.80 A; A=25-235.
DR PDBsum; 1BVB; -.
DR PDBsum; 1FT5; -.
DR PDBsum; 1FT6; -.
DR AlphaFoldDB; Q57142; -.
DR SMR; Q57142; -.
DR STRING; 228410.NE0960; -.
DR EnsemblBacteria; CAD84871; CAD84871; NE0960.
DR EnsemblBacteria; CAD85953; CAD85953; NE2042.
DR EnsemblBacteria; CAD86249; CAD86249; NE2337.
DR KEGG; neu:NE0960; -.
DR KEGG; neu:NE2042; -.
DR KEGG; neu:NE2337; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_1179215_0_0_4; -.
DR OMA; HYKLEGV; -.
DR OrthoDB; 738283at2; -.
DR PhylomeDB; Q57142; -.
DR BioCyc; MetaCyc:MON-17537; -.
DR EvolutionaryTrace; Q57142; -.
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 InterPro; IPR023155; Cyt_c-552/4.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF13435; Cytochrome_C554; 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..24
FT CHAIN 25..235
FT /note="Cytochrome c-554"
FT /evidence="ECO:0000269|PubMed:9808046"
FT /id="PRO_0000006543"
FT REGION 121..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9808046"
FT BINDING 38
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9808046"
FT BINDING 39
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 BINDING 51
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 BINDING 84
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 87
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 88
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 BINDING 112
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9808046"
FT BINDING 115
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9808046"
FT BINDING 116
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 BINDING 126
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 BINDING 158
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9808046"
FT BINDING 161
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9808046"
FT BINDING 162
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 BINDING 203
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 HELIX 33..38
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:1FT5"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1FT5"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1FT5"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1FT5"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1FT5"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:1FT5"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:1FT5"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1FT5"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1FT5"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:1FT5"
SQ SEQUENCE 235 AA; 25999 MW; 105961D14597554D CRC64;
MKIMIACGLV AAALFTLTSG QSLAADAPFE GRKKCSSCHK AQAQSWKDTA HAKAMESLKP
NVKKEAKQKA KLDPAKDYTQ DKDCVGCHVD GFGQKGGYTI ESPKPMLTGV GCESCHGPGR
NFRGDHRKSG QAFEKSGKKT PRKDLAKKGQ DFHFEERCSA CHLNYEGSPW KGAKAPYTPF
TPEVDAKYTF KFDEMVKEVK AMHEHYKLEG VFEGEPKFKF HDEFQASAKP AKKGK
