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Database: UniProt
Entry: B2FL46_STRMK
LinkDB: B2FL46_STRMK
Original site: B2FL46_STRMK 
ID   B2FL46_STRMK            Unreviewed;       308 AA.
AC   B2FL46;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Cytochrome c family protein {ECO:0000313|EMBL:CAQ45279.1};
GN   OrderedLocusNames=Smlt1757 {ECO:0000313|EMBL:CAQ45279.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ45279.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ45279.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ45279.1,
RC   ECO:0000313|Proteomes:UP000008840};
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR   EMBL; AM743169; CAQ45279.1; -; Genomic_DNA.
DR   RefSeq; WP_012479747.1; NC_010943.1.
DR   AlphaFoldDB; B2FL46; -.
DR   EnsemblBacteria; CAQ45279; CAQ45279; Smlt1757.
DR   KEGG; sml:Smlt1757; -.
DR   PATRIC; fig|522373.3.peg.1679; -.
DR   eggNOG; COG3258; Bacteria.
DR   HOGENOM; CLU_058582_2_0_6; -.
DR   Proteomes; UP000008840; Chromosome.
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; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR35008:SF4; SOXD PROTEIN; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF21342; SoxA-TsdA_cyt-c; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000008840}.
FT   DOMAIN          72..173
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          193..286
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          287..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  33509 MW;  F3D83C701076FB81 CRC64;
     MKRSRKRFRL LIGSAITLVM LAGAGTLAYR HLFPDLDAAV ASTIDILDAQ GKVVGHYHAP
     SAEEITGLGN AESVMLGRRI LNETARLLPD NVGNDLNCNS CHMAEGKRPF GNHYFNTGGG
     AYPRYMPRPG KVIGLTERIN GCLQRSMNGK PLPKDSPQMR AMLDYMAWLS SPVPEGAKVA
     APSEGPIDST LTPDPIRGQA LYAVQCAACH GDNGEGRRDA SGDIAFPPLW GDHSFNIGAG
     MARLYKATGF VKHNMPPAVT REPPLGQQMM PDQDAVDIAS YFINQPRPDF ANKAKDWPRD
     PKPKDARY
//
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