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Database: UniProt
Entry: G8PPW0_PSEUV
LinkDB: G8PPW0_PSEUV
Original site: G8PPW0_PSEUV 
ID   G8PPW0_PSEUV            Unreviewed;       152 AA.
AC   G8PPW0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Monoheme cytochrome c SoxX {ECO:0000313|EMBL:AEV35879.1};
GN   Name=soxX {ECO:0000313|EMBL:AEV35879.1};
GN   OrderedLocusNames=PSE_1367 {ECO:0000313|EMBL:AEV35879.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV35879.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV35879.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV35879.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
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DR   EMBL; CP003147; AEV35879.1; -; Genomic_DNA.
DR   RefSeq; WP_014284149.1; NC_016642.1.
DR   AlphaFoldDB; G8PPW0; -.
DR   STRING; 911045.PSE_1367; -.
DR   KEGG; psf:PSE_1367; -.
DR   eggNOG; COG2010; Bacteria.
DR   HOGENOM; CLU_114042_0_0_5; -.
DR   OMA; TVMPAFY; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProt.
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   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR030999; Thiosulf_SoxX.
DR   NCBIfam; TIGR04485; thiosulf_SoxX; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..152
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003513884"
FT   DOMAIN          45..151
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   152 AA;  16043 MW;  258C253283EB9109 CRC64;
     MKAIAKTIAA ATLLISGSAV AGVVAPGDVQ FVEAAVPVSL TGVAGDPAKG REWFANRKLG
     NCLACHANDD LEEEQFHGEI GPYLEGIGDT YSEAELRAIV INSKEVFGDA TIMPAFYKTD
     GLNRVAKKFA GKTILSAEQV EDIVAYLATL KE
//
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