SHP_CERS4
ID SHP_CERS4 Reviewed; 129 AA.
AC P81238; Q3J4W2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cytochrome c-type protein SHP;
DE AltName: Full=Oxygen-binding heme protein;
DE AltName: Full=Sphaeroides heme protein;
DE Flags: Precursor;
GN Name=shp; OrderedLocusNames=RHOS4_06040; ORFNames=RSP_2021;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 18-129.
RX PubMed=9558336; DOI=10.1021/bi972498w;
RA Klarskov K., van Driessche G., Backers K., Dumortier C., Meyer T.E.,
RA Tollin G., Cusanovich M.A., van Beeumen J.J.;
RT "Ligand binding and covalent structure of an oxygen-binding heme protein
RT from Rhodobacter sphaeroides, a representative of a new structural family
RT of c-type cytochromes.";
RL Biochemistry 37:5995-6002(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 18-129.
RX PubMed=10821858; DOI=10.1074/jbc.275.21.16050;
RA Leys D., Backers K., Meyer T.E., Hagen W.R., Cusanovich M.A.,
RA Van Beeumen J.J.;
RT "Crystal structures of an oxygen-binding cytochrome c from Rhodobacter
RT sphaeroides.";
RL J. Biol. Chem. 275:16050-16056(2000).
CC -!- FUNCTION: High-spin cytochrome. Transiently bind oxygen during
CC autoxidation, which occurs with a half-life of 3 min with a 4-fold
CC excess of O(2). Also binds carbon monoxide, azide and cyanide.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -22 mV.;
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; CP000143; ABA78172.1; -; Genomic_DNA.
DR RefSeq; WP_011337164.1; NZ_CP030271.1.
DR RefSeq; YP_352073.1; NC_007493.2.
DR PDB; 1DW0; X-ray; 1.82 A; A/B/C=18-129.
DR PDB; 1DW1; X-ray; 1.90 A; A/B/C=18-129.
DR PDB; 1DW2; X-ray; 2.20 A; A/B/C=18-129.
DR PDB; 1DW3; X-ray; 2.10 A; A/B/C=18-129.
DR PDBsum; 1DW0; -.
DR PDBsum; 1DW1; -.
DR PDBsum; 1DW2; -.
DR PDBsum; 1DW3; -.
DR AlphaFoldDB; P81238; -.
DR SMR; P81238; -.
DR STRING; 272943.RSP_2021; -.
DR EnsemblBacteria; ABA78172; ABA78172; RSP_2021.
DR KEGG; rsp:RSP_2021; -.
DR PATRIC; fig|272943.9.peg.913; -.
DR eggNOG; COG1858; Bacteria.
DR OMA; TEKWFRR; -.
DR PhylomeDB; P81238; -.
DR EvolutionaryTrace; P81238; -.
DR Proteomes; UP000002703; Chromosome 1.
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 InterPro; IPR015170; DUF1924.
DR Pfam; PF09086; DUF1924; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Heme; Iron; Metal-binding; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:9558336"
FT CHAIN 18..129
FT /note="Cytochrome c-type protein SHP"
FT /id="PRO_0000045861"
FT BINDING 60
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 63
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 64
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 DISULFID 106..114
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:1DW0"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:1DW0"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1DW0"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1DW0"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1DW0"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:1DW0"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:1DW0"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:1DW0"
SQ SEQUENCE 129 AA; 13283 MW; A52D8740F2CC4917 CRC64;
MTRFLILSAV LAGPALAGDT SPAQLIAGYE AAAGAPADAE RGRALFLSTQ TGGKPDTPSC
TTCHGADVTR AGQTRTGKEI APLAPSATPD RFTDSARVEK WLGRNCNSVI GRDCTPGEKA
DLLAWLAAQ
