ID Q3K5E5_PSEPF Unreviewed; 149 AA.
AC Q3K5E5;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Putative exported cytochrome C {ECO:0000313|EMBL:ABA77009.1};
GN OrderedLocusNames=Pfl01_5272 {ECO:0000313|EMBL:ABA77009.1};
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA77009.1, ECO:0000313|Proteomes:UP000002704};
RN [1] {ECO:0000313|EMBL:ABA77009.1, ECO:0000313|Proteomes:UP000002704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA77009.1,
RC ECO:0000313|Proteomes:UP000002704};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR000027-2}.
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DR EMBL; CP000094; ABA77009.1; -; Genomic_DNA.
DR RefSeq; WP_011336332.1; NC_007492.2.
DR AlphaFoldDB; Q3K5E5; -.
DR KEGG; pfo:Pfl01_5272; -.
DR eggNOG; COG3909; Bacteria.
DR HOGENOM; CLU_106713_4_0_6; -.
DR Proteomes; UP000002704; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..149
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004226851"
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; 16389 MW; 0F273755856A33C7 CRC64;
MTLKRISVVL LACLTLSACG GVDPNSPLGQ RKAIFKQMLK TGEDLGGMLR GRIAFDGPKF
AEGAVKLDAL SHEPWKHFPQ VREEDHTSAK DDVWQKQARF QEMARSLEAA TGELVIASKV
QPYKASNLGP AVQKVEDACS ACHKEFRDH
//
