CY552_MARNT
ID CY552_MARNT Reviewed; 88 AA.
AC P82903;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytochrome c-552;
DE AltName: Full=Cytochrome c552;
OS Marinobacter nauticus (Marinobacter hydrocarbonoclasticus) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=2743;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=617;
RX PubMed=7925398; DOI=10.1111/j.1432-1033.1994.01011.x;
RA Saraiva L.M., Fauque G., Besson S., Moura I.;
RT "Physico-chemical and spectroscopic properties of the monohemic cytochrome
RT C552 from Pseudomonas nautica 617.";
RL Eur. J. Biochem. 224:1011-1017(1994).
RN [2]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC STRAIN=617;
RX PubMed=15674861; DOI=10.1002/jms.788;
RA Di Tullio A., Caputi L., Malatesta F., Reale S., De Angelis F.;
RT "Characterization of a novel microperoxidase from Marinobacter
RT hydrocarbonoclasticus by electrospray ionization tandem mass
RT spectrometry.";
RL J. Mass Spectrom. 40:325-330(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND MASS SPECTROMETRY.
RC STRAIN=617;
RX PubMed=10369779; DOI=10.1006/jmbi.1999.2838;
RA Brown K., Nurizzo D., Besson S., Shepard W., Moura J., Moura I., Tegoni M.,
RA Cambillau C.;
RT "MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the
RT c4 dihemic cytochrome domain association.";
RL J. Mol. Biol. 289:1017-1028(1999).
CC -!- FUNCTION: Electron donor for periplasmic nitrate reductase.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- MASS SPECTROMETRY: Mass=9466; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10369779};
CC -!- MASS SPECTROMETRY: Mass=9463.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15674861};
CC -!- MASS SPECTROMETRY: Mass=9463.3; Mass_error=0.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15674861};
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR PDB; 1CNO; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-84.
DR PDBsum; 1CNO; -.
DR AlphaFoldDB; P82903; -.
DR SMR; P82903; -.
DR EvolutionaryTrace; P82903; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF00034; Cytochrom_C; 1.
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; Transport.
FT CHAIN 1..88
FT /note="Cytochrome c-552"
FT /id="PRO_0000108400"
FT BINDING 14
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 17
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 18
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 BINDING 60
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 CONFLICT 36
FT /note="K -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 79..88
FT /note="YASLPADGQG -> GASXP (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:1CNO"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1CNO"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1CNO"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:1CNO"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:1CNO"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:1CNO"
SQ SEQUENCE 88 AA; 8847 MW; CE8EFEEB691AB2E0 CRC64;
AGDIEAGKAK AAVCAACHGQ NGISQVPIYP NLAGQKEQYL VAALKAYKAG QRQGGQAPVM
QGQATALSDA DIANLAAYYA SLPADGQG
