CY551_PSEST
ID CY551_PSEST Reviewed; 104 AA.
AC P00101; P24036;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cytochrome c-551;
DE AltName: Full=Cytochrome C8;
DE AltName: Full=Cytochrome c551;
DE Flags: Precursor;
GN Name=nirM;
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX PubMed=2001732; DOI=10.1016/0014-5793(91)80150-2;
RA Juengst A., Wakabayashi S., Matsubara H., Zumft W.G.;
RT "The nirSTBM region coding for cytochrome cd1-dependent nitrite respiration
RT of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme
RT proteins.";
RL FEBS Lett. 279:205-209(1991).
RN [2]
RP PROTEIN SEQUENCE OF 23-104.
RC STRAIN=221;
RX PubMed=4352718; DOI=10.1042/bj1310485;
RA Ambler R.P., Wynn M.;
RT "The amino acid sequences of cytochromes c-551 from three species of
RT Pseudomonas.";
RL Biochem. J. 131:485-498(1973).
RN [3]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC 17588 / LMG 11199 / NCIMB 11358 / Stanier 221;
RX PubMed=1327105; DOI=10.1021/bi00151a030;
RA Cai M., Bradford E.G., Timkovich R.;
RT "Investigation of the solution conformation of cytochrome c-551 from
RT Pseudomonas stutzeri.";
RL Biochemistry 31:8603-8612(1992).
RN [4]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX PubMed=7811935; DOI=10.1016/s0006-3495(94)80590-9;
RA Cai M., Timkovich R.;
RT "Solution conformation of cytochrome c-551 from Pseudomonas stutzeri ZoBell
RT determined by NMR.";
RL Biophys. J. 67:1207-1215(1994).
CC -!- FUNCTION: Electron donor for cytochrome cd1 in nitrite and nitrate
CC respiration.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; X53676; CAA40153.1; -; Genomic_DNA.
DR PIR; A00093; CCPS5S.
DR PIR; S13939; CCPS5B.
DR RefSeq; WP_003279940.1; NZ_PPXG01000004.1.
DR PDB; 1CCH; NMR; -; A=23-104.
DR PDB; 1COR; NMR; -; A=24-104.
DR PDB; 1FI3; NMR; -; A=23-104.
DR PDB; 2I8F; NMR; -; A=23-104.
DR PDBsum; 1CCH; -.
DR PDBsum; 1COR; -.
DR PDBsum; 1FI3; -.
DR PDBsum; 2I8F; -.
DR AlphaFoldDB; P00101; -.
DR BMRB; P00101; -.
DR SMR; P00101; -.
DR STRING; 32042.PstZobell_00952; -.
DR DrugBank; DB03317; Ferroheme C.
DR EvolutionaryTrace; P00101; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002324; Cyt_c_ID.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PRINTS; PR00606; CYTCHROMECID.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:4352718"
FT CHAIN 23..104
FT /note="Cytochrome c-551"
FT /id="PRO_0000006528"
FT BINDING 34
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 37
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 38
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT VARIANT 40
FT /note="V -> I (in strain: 221)"
FT VARIANT 42
FT /note="T -> A (in strain: 221)"
FT VARIANT 44
FT /note="M -> L (in strain: 221)"
FT VARIANT 49
FT /note="L -> F (in strain: 221)"
FT VARIANT 56
FT /note="N -> Y (in strain: 221)"
FT VARIANT 59..60
FT /note="VE -> QD (in strain: 221)"
FT VARIANT 65
FT /note="T -> L (in strain: 221)"
FT VARIANT 68
FT /note="L -> G (in strain: 221)"
FT VARIANT 100
FT /note="V -> I (in strain: 221)"
FT VARIANT 103
FT /note="L -> Q (in strain: 221)"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:1CCH"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1CCH"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1CCH"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1CCH"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1CCH"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1CCH"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1CCH"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:1CCH"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1CCH"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:1CCH"
SQ SEQUENCE 104 AA; 10797 MW; CF21CAE20D6CD95D CRC64;
MKKILIPMLA LGGALAMQPA LAQDGEALFK SKPCAACHSV DTKMVGPALK EVAAKNAGVE
GAADTLALHI KNGSQGVWGP IPMPPNPVTE EEAKILAEWV LSLK
