CY551_PSEAE
ID CY551_PSEAE Reviewed; 104 AA.
AC P00099;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cytochrome c-551;
DE AltName: Full=Cytochrome C8;
DE AltName: Full=Cytochrome c551;
DE Flags: Precursor;
GN Name=nirM; OrderedLocusNames=PA0518;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NBRC 12689 / NCIMB
RC 8295 / NRRL B-771;
RX PubMed=2152881; DOI=10.1016/0014-5793(90)80015-b;
RA Nordling M., Young S., Karlsson B.G., Lundberg L.G.;
RT "The structural gene for cytochrome c551 from Pseudomonas aeruginosa. The
RT nucleotide sequence shows a location downstream of the nitrite reductase
RT gene.";
RL FEBS Lett. 259:230-232(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2155133; DOI=10.1016/0014-5793(90)80669-a;
RA Arai H., Sanbongi Y., Igarashi Y., Kodama T.;
RT "Cloning and sequencing of the gene encoding cytochrome c-551 from
RT Pseudomonas aeruginosa.";
RL FEBS Lett. 261:196-198(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP PROTEIN SEQUENCE OF 23-104.
RC STRAIN=P6009;
RX PubMed=14084622; DOI=10.1042/bj0890349;
RA Ambler R.P.;
RT "The amino acid sequence of Pseudomonas cytochrome c-551.";
RL Biochem. J. 89:349-378(1963).
RN [5]
RP PROTEIN SEQUENCE OF 23-104.
RC STRAIN=Various strains;
RX PubMed=4362497; DOI=10.1042/bj1370003;
RA Ambler R.P.;
RT "The evolutionary stability of cytochrome c-551 in Pseudomonas aeruginosa
RT and Pseudomonas fluorescens biotype C.";
RL Biochem. J. 137:3-14(1974).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=6283101; DOI=10.1016/0022-2836(82)90335-7;
RA Matsuura Y., Takano T., Dickerson R.E.;
RT "Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6-A
RT resolution and comparison of the two redox forms.";
RL J. Mol. Biol. 156:389-409(1982).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=96440; DOI=10.1073/pnas.75.6.2674;
RA Almassy R.J., Dickerson R.E.;
RT "Pseudomonas cytochrome c551 at 2.0-A resolution: enlargement of the
RT cytochrome c family.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:2674-2678(1978).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=2174259; DOI=10.1021/bi00492a011;
RA Detlefsen D.J., Thanabal V., Pecoraro V.L., Wagner G.;
RT "Sequential 1H NMR assignments of iron(II) cytochrome c551 from Pseudomonas
RT aeruginosa.";
RL Biochemistry 29:9377-9386(1990).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=1654086; DOI=10.1021/bi00101a019;
RA Detlefsen D.J., Thanabal V., Pecoraro V.L., Wagner G.;
RT "Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa
RT as determined by two-dimensional 1H NMR.";
RL Biochemistry 30:9040-9046(1991).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=8218218; DOI=10.1021/bi00094a007;
RA Timkovich R., Cai M.;
RT "Investigation of the structure of oxidized Pseudomonas aeruginosa
RT cytochrome c-551 by NMR: comparison of observed paramagnetic shifts and
RT calculated pseudocontact shifts.";
RL Biochemistry 32:11516-11523(1993).
CC -!- FUNCTION: Electron donor for cytochrome cd1 in nitrite and nitrate
CC respiration.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is about +260 mV.;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; X51319; CAA35703.1; -; Genomic_DNA.
DR EMBL; X51631; CAA35958.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03907.1; -; Genomic_DNA.
DR PIR; B34141; CCPS5A.
DR RefSeq; NP_249209.1; NC_002516.2.
DR RefSeq; WP_003084872.1; NZ_QZGE01000010.1.
DR PDB; 1DVV; NMR; -; A=23-104.
DR PDB; 2EXV; X-ray; 1.86 A; A/C=23-104.
DR PDB; 2PAC; NMR; -; A=23-104.
DR PDB; 351C; X-ray; 1.60 A; A=23-104.
DR PDB; 3X39; X-ray; 1.50 A; A/B=23-104.
DR PDB; 451C; X-ray; 1.60 A; A=23-104.
DR PDB; 5XEC; X-ray; 1.10 A; A=23-42, C=43-104.
DR PDB; 5XED; X-ray; 1.55 A; A=23-42, C=43-104.
DR PDBsum; 1DVV; -.
DR PDBsum; 2EXV; -.
DR PDBsum; 2PAC; -.
DR PDBsum; 351C; -.
DR PDBsum; 3X39; -.
DR PDBsum; 451C; -.
DR PDBsum; 5XEC; -.
DR PDBsum; 5XED; -.
DR AlphaFoldDB; P00099; -.
DR BMRB; P00099; -.
DR SMR; P00099; -.
DR STRING; 287.DR97_3486; -.
DR PaxDb; P00099; -.
DR PRIDE; P00099; -.
DR DNASU; 882220; -.
DR EnsemblBacteria; AAG03907; AAG03907; PA0518.
DR GeneID; 882220; -.
DR KEGG; pae:PA0518; -.
DR PATRIC; fig|208964.12.peg.548; -.
DR PseudoCAP; PA0518; -.
DR HOGENOM; CLU_133112_1_0_6; -.
DR InParanoid; P00099; -.
DR OMA; MGPALHD; -.
DR BioCyc; PAER208964:G1FZ6-523-MON; -.
DR EvolutionaryTrace; P00099; -.
DR Proteomes; UP000002438; Chromosome.
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; Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:14084622,
FT ECO:0000269|PubMed:4362497"
FT CHAIN 23..104
FT /note="Cytochrome c-551"
FT /evidence="ECO:0000269|PubMed:2152881"
FT /id="PRO_0000006527"
FT BINDING 34
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 37
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
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 ECO:0000269|PubMed:6283101"
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 ECO:0000269|PubMed:6283101"
FT VARIANT 24
FT /note="D -> A (in strain: 129/1224)"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:5XEC"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5XEC"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:351C"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:5XEC"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:5XEC"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5XEC"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:5XEC"
SQ SEQUENCE 104 AA; 10967 MW; 3AA94749BCEE4A94 CRC64;
MKPYALLSLL ATGTLLAQGA WAEDPEVLFK NKGCVACHAI DTKMVGPAYK DVAAKFAGQA
GAEAELAQRI KNGSQGVWGP IPMPPNAVSD DEAQTLAKWV LSQK