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Database: UniProt
Entry: A0A2S9KEI5_9BURK
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ID   A0A2S9KEI5_9BURK        Unreviewed;       149 AA.
AC   A0A2S9KEI5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Cytochrome C {ECO:0000313|EMBL:PRD68847.1};
GN   ORFNames=C6P61_08925 {ECO:0000313|EMBL:PRD68847.1};
OS   Malikia spinosa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Malikia.
OX   NCBI_TaxID=86180 {ECO:0000313|EMBL:PRD68847.1, ECO:0000313|Proteomes:UP000238326};
RN   [1] {ECO:0000313|EMBL:PRD68847.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=83 {ECO:0000313|EMBL:PRD68847.1};
RA   Suzuki S., Ishii S., Walworth N., Bird L., Kuenen J.G., Nealson K.H.;
RT   "Comparative genomics illustrates the genes involved in a hyperalkaliphilic
RT   mechanisms of Serpentinomonas isolated from highly-alkaline calcium-rich
RT   serpentinized springs.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR000027-2}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRD68847.1}.
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DR   EMBL; PVLR01000023; PRD68847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9KEI5; -.
DR   OrthoDB; 5520910at2; -.
DR   Proteomes; UP000238326; Unassembled WGS sequence.
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   Gene3D; 1.20.120.10; Cytochrome c/b562; 1.
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; Cytochromes; 1.
DR   PROSITE; PS51009; CYTCII; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000027-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000027-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000027-1}; Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..149
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015691964"
FT   BINDING         139
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT   BINDING         142
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT   BINDING         143
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:0000256|PIRSR:PIRSR000027-1"
SQ   SEQUENCE   149 AA;  15734 MW;  7D403B460DD72FC3 CRC64;
     MKVRHALMLA AAMLSAGAAQ AQFQKPEDAV KYRQSAFSVM GTHFARLGAM ANGKVPFDAK
     KAQEDAAVVL MLSRLPWAGF TPDTQQLESK AKPALWSEMD KVKGGADKLM TAAVALDAAA
     KTGSLDAVKK TFGDAAASCK ACHDAYKSK
//
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