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Database: UniProt
Entry: A0A2Z6E781_9GAMM
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ID   A0A2Z6E781_9GAMM        Unreviewed;       237 AA.
AC   A0A2Z6E781;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Cytochrome c4 {ECO:0000313|EMBL:BBD80877.1};
GN   ORFNames=ALSL_2251 {ECO:0000313|EMBL:BBD80877.1};
OS   Aerosticca soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Aerosticca.
OX   NCBI_TaxID=2010829 {ECO:0000313|EMBL:BBD80877.1, ECO:0000313|Proteomes:UP000270530};
RN   [1] {ECO:0000313|Proteomes:UP000270530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dysh456 {ECO:0000313|Proteomes:UP000270530};
RA   Watanabe M., Kojima H.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000270530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dysh456 {ECO:0000313|Proteomes:UP000270530};
RA   Fukui M.;
RT   "Genome sequence of Rhodanobacteraceae bacterium strain Dysh456.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- PTM: Binds 2 heme c groups covalently per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000005-1}.
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DR   EMBL; AP018560; BBD80877.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6E781; -.
DR   KEGG; rbd:ALSL_2251; -.
DR   OrthoDB; 9773456at2; -.
DR   Proteomes; UP000270530; Chromosome.
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:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR024167; Cytochrome_c4-like.
DR   PANTHER; PTHR33751; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR   PANTHER; PTHR33751:SF9; CYTOCHROME C4; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000005-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000005-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000005-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270530};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..237
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016328739"
FT   DOMAIN          47..125
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          133..237
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         59
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         62
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         63
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         102
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         154
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         157
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         158
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         215
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
SQ   SEQUENCE   237 AA;  24563 MW;  5BAB2838A0BD1368 CRC64;
     MNYASTVLLA LLAAAPIAAF AQEASPPAGT GTPTGFMDVR AIRPVAGDAK AGAGKVTICS
     ACHGHSGMAV VPELGNLAGQ PATYLYIQLK AFKDGYRSDP VMSGQAARLS DEDMRDIAAY
     YASFAPASHG GTDTSSPGAR LYREGDPGRG IPPCQGCHGP DARGPRPFVA DVEGKPQPPW
     FTYPYLHGQS ANFVTKALGD FRAGVRAGTS NARIMQGVAQ GLSDADIQAL SAYLPHL
//
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