ID G7ZER5_AZOL4 Unreviewed; 253 AA.
AC G7ZER5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Cytochrome c1 {ECO:0000256|ARBA:ARBA00016165};
GN Name=petC {ECO:0000313|EMBL:CBS90322.1};
GN OrderedLocusNames=AZOLI_p30507 {ECO:0000313|EMBL:CBS90322.1};
OS Azospirillum lipoferum (strain 4B).
OG Plasmid AZO_p3 {ECO:0000313|EMBL:CBS90322.1,
OG ECO:0000313|Proteomes:UP000005667}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS90322.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC PLASMID=Plasmid AZO_p3 {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR602326-1};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602326-1};
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DR EMBL; FQ311871; CBS90322.1; -; Genomic_DNA.
DR RefSeq; WP_014249759.1; NC_016623.1.
DR AlphaFoldDB; G7ZER5; -.
DR KEGG; ali:AZOLI_p30507; -.
DR HOGENOM; CLU_040334_1_2_5; -.
DR OrthoDB; 9808471at2; -.
DR Proteomes; UP000005667; Plasmid AZO_p3.
DR GO; GO:0016020; C:membrane; 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; Cytochrome c-like domain; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR InterPro; IPR021157; Cyt_c1_TM_anchor_C.
DR PANTHER; PTHR10266; CYTOCHROME C1; 1.
DR PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF81496; Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602326-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602326-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602326-1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Plasmid {ECO:0000313|EMBL:CBS90322.1}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..253
FT /note="Cytochrome c1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003507089"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..176
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 59
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 62
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 63
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 182
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
SQ SEQUENCE 253 AA; 27141 MW; CB4A3B464540360F CRC64;
MRALKTAILS AALALGIAGA AQASEAVHIP KQNWPHSGIF GTIDKASAQR GFQIYKEVCA
ACHSMRLVPI RTLAGIGFSE DELKAIAAGY EVQAGPNDAG EMFMRPAIPA DRFPSPFANE
QAARASNNGA LPPDLSLMAK ARVGGEDYLY AFLTGFEEPP ADVKLMDGMS YNKVFPGHQV
GMPNILQPDG VTFADGTKAT VEQQAHDVAT FLTFAAEPHL DARKQMGVKV ILFLLVLAGL
MYATKRKLWS TLH
//