ID Q0VLG1_ALCBS Unreviewed; 119 AA.
AC Q0VLG1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Cytochrome c5, putative {ECO:0000313|EMBL:CAL17987.1};
GN OrderedLocusNames=ABO_2539 {ECO:0000313|EMBL:CAL17987.1};
OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS SK2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=393595 {ECO:0000313|EMBL:CAL17987.1, ECO:0000313|Proteomes:UP000008871};
RN [1] {ECO:0000313|EMBL:CAL17987.1, ECO:0000313|Proteomes:UP000008871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2
RC {ECO:0000313|Proteomes:UP000008871};
RX PubMed=16878126; DOI=10.1038/nbt1232;
RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA Weidner S., Kaiser O., Golyshin P.N.;
RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT Alcanivorax borkumensis.";
RL Nat. Biotechnol. 24:997-1004(2006).
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DR EMBL; AM286690; CAL17987.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0VLG1; -.
DR STRING; 393595.ABO_2539; -.
DR KEGG; abo:ABO_2539; -.
DR eggNOG; COG3245; Bacteria.
DR HOGENOM; CLU_082349_3_1_6; -.
DR Proteomes; UP000008871; Chromosome.
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; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002323; Cyt_CIE.
DR PANTHER; PTHR40942; -; 1.
DR PANTHER; PTHR40942:SF4; CYTOCHROME C5; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PRINTS; PR00607; CYTCHROMECIE.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 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|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:UP000008871};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..119
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004178739"
FT DOMAIN 33..116
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 119 AA; 12961 MW; 0EEA0743ECC04959 CRC64;
MQKLYWYSIA MVLPVLWLAG CSDDSAPANG PAQQARDGAQ LYRQYCVTCH GSGALGAPGV
GKEHRPYWSH EIEEDGFDAL VLDAINGFNS MPPRGGCFDC SDDEIRSTVI YMLNKSGAK
//
