ID   C554_METTR              Reviewed;         132 AA.
AC   D5QVH0;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Cytochrome c-554 {ECO:0000303|PubMed:21789203};
DE   AltName: Full=Cytochrome c class I {ECO:0000312|EMBL:EFH01442.1};
DE   Flags: Precursor;
GN   ORFNames=MettrDRAFT_3796;
OS   Methylosinus trichosporium.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylocystaceae; Methylosinus.
OX   NCBI_TaxID=426;
RN   [1] {ECO:0000312|EMBL:EFH01442.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC   {ECO:0000312|EMBL:EFH01442.1};
RX   PubMed=20952571; DOI=10.1128/jb.01144-10;
RA   Stein L.Y., Yoon S., Semrau J.D., Dispirito A.A., Murrell J.C.,
RA   Vuilleumier S., Kalyuzhnaya M.G., Op den Camp H.J., Bringel F., Bruce D.,
RA   Cheng J.F., Copeland A., Goodwin L., Han S., Hauser L., Jetten M.S.,
RA   Lajus A., Land M.L., Lapidus A., Lucas S., Medigue C., Pitluck S.,
RA   Woyke T., Zeytun A., Klotz M.G.;
RT   "Genome sequence of the obligate methanotroph Methylosinus trichosporium
RT   strain OB3b.";
RL   J. Bacteriol. 192:6497-6498(2010).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 25-63 AND 104-132, SUBCELLULAR LOCATION, PTM, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC   {ECO:0000269|PubMed:21789203};
RX   PubMed=21789203; DOI=10.1371/journal.pone.0022014;
RA   Harbitz E., Andersson K.K.;
RT   "Cytochrome c-554 from Methylosinus trichosporium OB3b; a protein that
RT   belongs to the cytochrome c2 family and exhibits a HALS-Type EPR signal.";
RL   PLoS ONE 6:E22014-E22014(2011).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000303|PubMed:21789203}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC       {ECO:0000269|PubMed:21789203}.
CC   -!- MASS SPECTROMETRY: Mass=12230; Mass_error=15; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21789203};
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DR   EMBL; ADVE01000068; EFH01442.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5QVH0; -.
DR   SMR; D5QVH0; -.
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   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Periplasm; Signal; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:21789203"
FT   CHAIN           25..132
FT                   /note="Cytochrome c-554"
FT                   /evidence="ECO:0000269|PubMed:21789203"
FT                   /id="PRO_0000419255"
FT   DOMAIN          26..126
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         38
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P00085,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         41
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P00085,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         42
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:0000250|UniProtKB:P00085,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         104
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:0000250|UniProtKB:P00085,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   132 AA;  13932 MW;  B686DD1FBF712484 CRC64;
     MKSISMLTLA ASVAFAVTAG QAVAAGDPAA GEKVFNKCKA CHQVGETAKN AVAPELNGID
     GRKSASAEGY NYSEPFKALG ITWDEAQFKE FIKNPKAKVP GTKMIFPGLS SENDQANVWA
     YLSQFGADGK KK