位置:首页 > 蛋白库 > C556_RHOPA
C556_RHOPA
ID   C556_RHOPA              Reviewed;         149 AA.
AC   P00150;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Cytochrome c-556;
DE   AltName: Full=Cytochrome c556;
DE   Flags: Precursor;
GN   OrderedLocusNames=RPA3973;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-149.
RC   STRAIN=ATCC 17007 / ATH 2.1.37 / NCIB 11774;
RX   PubMed=6273892; DOI=10.1073/pnas.78.11.6854;
RA   Ambler R.P., Bartsch R.G., Daniel M., Kamen M.D., McLellan L., Meyer T.E.,
RA   van Beeumen J.;
RT   "Amino acid sequences of bacterial cytochromes c' and c-556.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:6854-6857(1981).
CC   -!- FUNCTION: Low-spin monoheme cytochrome c.
CC   -!- SUBUNIT: Monomer.
CC   -!- PTM: Binds 1 heme group 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; BX572605; CAE29414.1; -; Genomic_DNA.
DR   PIR; A00143; CCRF6P.
DR   RefSeq; WP_011159509.1; NC_005296.1.
DR   PDB; 1S05; NMR; -; A=21-149.
DR   PDBsum; 1S05; -.
DR   AlphaFoldDB; P00150; -.
DR   SMR; P00150; -.
DR   STRING; 258594.RPA3973; -.
DR   PRIDE; P00150; -.
DR   EnsemblBacteria; CAE29414; CAE29414; RPA3973.
DR   GeneID; 66895089; -.
DR   KEGG; rpa:RPA3973; -.
DR   eggNOG; COG3909; Bacteria.
DR   HOGENOM; CLU_106713_2_0_5; -.
DR   OMA; HYRQSAF; -.
DR   PhylomeDB; P00150; -.
DR   BioCyc; RPAL258594:TX73_RS20280-MON; -.
DR   EvolutionaryTrace; P00150; -.
DR   Proteomes; UP000001426; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
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   InterPro; IPR010980; Cyt_c/b562.
DR   InterPro; IPR002321; Cyt_c_II.
DR   InterPro; IPR012127; Cyt_c_prime.
DR   Pfam; PF01322; Cytochrom_C_2; 1.
DR   PIRSF; PIRSF000027; Cytc_c_prime; 1.
DR   SUPFAM; SSF47175; SSF47175; 1.
DR   PROSITE; PS51009; CYTCII; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Metal-binding; Reference proteome; Signal; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:6273892"
FT   CHAIN           21..149
FT                   /note="Cytochrome c-556"
FT                   /id="PRO_0000006548"
FT   BINDING         40
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         137
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT   BINDING         140
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT   BINDING         141
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   HELIX           25..47
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   HELIX           55..66
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   HELIX           99..119
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   HELIX           123..129
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   TURN            130..134
FT                   /evidence="ECO:0007829|PDB:1S05"
FT   HELIX           135..143
FT                   /evidence="ECO:0007829|PDB:1S05"
SQ   SEQUENCE   149 AA;  16149 MW;  6748A28E762AA1C6 CRC64;
     MLRTVIVAGA LVLTASAVMA QQDLVDKTQK LMKDNGRNMM VLGAIAKGEK PYDQAAVDAA
     LKQFDETAKD LPKLFPDSVK GLKPFDSKYS SSPKIWAERA KFDTEIADFA KAVDGAKGKI
     KDVDTLKAAM QPIGKACGNC HENFRDKEG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024