ID A4G801_HERAR Unreviewed; 277 AA.
AC A4G801;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Cytochrome c {ECO:0000313|EMBL:CAL62638.1};
GN OrderedLocusNames=HEAR2512 {ECO:0000313|EMBL:CAL62638.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL62638.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL62638.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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DR EMBL; CU207211; CAL62638.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G801; -.
DR STRING; 204773.HEAR2512; -.
DR KEGG; har:HEAR2512; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_065353_0_0_4; -.
DR OrthoDB; 9765171at2; -.
DR Proteomes; UP000006697; Chromosome.
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; Cytochrome c-like domain; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR PANTHER; PTHR37823; CYTOCHROME C-553-LIKE; 1.
DR PANTHER; PTHR37823:SF4; MENAQUINOL-CYTOCHROME C REDUCTASE CYTOCHROME B_C SUBUNIT; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002668073"
FT DOMAIN 186..274
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 277 AA; 30779 MW; 3B0FB402C56C58EE CRC64;
MKTLFSPAVR AFLLCMSAWL LCAAGNPAQA AEPVLELSFS KQQQRLTRAD LLRHPDVRTI
EVPADSAYKQ PMKYRALPLL SILRNVRDVD VLQFRAEDGF VANIPTALLS GGAQPWLAIE
PAHTPWPALK TGGRSAGPFY LVWLAPEKSG ITPELWPYQI AAISAVTPLQ NRYPQILPAA
SSAADSAEYR GMHIYTMQCA ACHQINGGGD ATVGPDLNLP FNPTEYFQGD FLRRYIRNPS
AVRSWPHMTM PGFSEQVLSE SQMDDLLAYL RHMTQRR
//
