ID A0A078LX04_9PSED Unreviewed; 210 AA.
AC A0A078LX04;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Cytochrome c4 {ECO:0000313|EMBL:CDZ94827.1, ECO:0000313|EMBL:RRV17355.1};
GN ORFNames=BN1079_02152 {ECO:0000313|EMBL:CDZ94827.1}, EGJ00_03245
GN {ECO:0000313|EMBL:RRV17355.1};
OS Pseudomonas saudiphocaensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ94827.1, ECO:0000313|Proteomes:UP000053902};
RN [1] {ECO:0000313|EMBL:CDZ94827.1, ECO:0000313|Proteomes:UP000053902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20_BN {ECO:0000313|EMBL:CDZ94827.1,
RC ECO:0000313|Proteomes:UP000053902};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRV17355.1, ECO:0000313|Proteomes:UP000271179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS_399 {ECO:0000313|EMBL:RRV17355.1,
RC ECO:0000313|Proteomes:UP000271179};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-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; CCSF01000001; CDZ94827.1; -; Genomic_DNA.
DR EMBL; RHQU01000002; RRV17355.1; -; Genomic_DNA.
DR RefSeq; WP_037024197.1; NZ_RHQU01000002.1.
DR AlphaFoldDB; A0A078LX04; -.
DR STRING; 1499686.BN1079_02152; -.
DR eggNOG; COG2863; Bacteria.
DR HOGENOM; CLU_076280_2_1_6; -.
DR OrthoDB; 9773456at2; -.
DR Proteomes; UP000053902; Unassembled WGS sequence.
DR Proteomes; UP000271179; Unassembled WGS sequence.
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; 2.
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:UP000053902};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..210
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035985784"
FT DOMAIN 22..109
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 118..210
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 34
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 37
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 38
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 86
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 139
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 142
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 143
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 187
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 210 AA; 21709 MW; 8F9AD67C332A215E CRC64;
MNKVLVSLLL TLGITGMAHA AGDAEAGSSK VAVCGACHGA DGNSPAPNFP KLAGQGEAYL
LKQLKDIKAG STPGAPEGEG RKVLEMTGML DPYSDQDLED IAAYFASQKG TVGMADPALV
ELGEKLFRGG KLELGMPSCT GCHSPNGAGN DLAGFPQLGG QHAAYTAKQL TDFREGNRTN
DGEAMIMRSI AAKLSNKDIE ALSSYIQGLH
//
