(data stored in SCRATCH zone)

SWISSPROT: C5BCT6_EDWI9

ID   C5BCT6_EDWI9            Unreviewed;       391 AA.
AC   C5BCT6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000014};
GN   OrderedLocusNames=NT01EI_0300 {ECO:0000313|EMBL:ACR67542.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67542.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|PIRNR:PIRNR000014}.
CC   -!- PTM: Binds 5 heme groups per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000014-1}.
CC   -!- SIMILARITY: Belongs to the TorC/TorY family.
CC       {ECO:0000256|PIRNR:PIRNR000014}.
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DR   EMBL; CP001600; ACR67542.1; -; Genomic_DNA.
DR   RefSeq; WP_015869751.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0300; -.
DR   EnsemblBacteria; ACR67542; ACR67542; NT01EI_0300.
DR   GeneID; 7960080; -.
DR   KEGG; eic:NT01EI_0300; -.
DR   PATRIC; fig|634503.3.peg.271; -.
DR   eggNOG; ENOG4105CUW; Bacteria.
DR   eggNOG; COG3005; LUCA.
DR   HOGENOM; HOG000284378; -.
DR   KO; K03532; -.
DR   OMA; MISRIWK; -.
DR   OrthoDB; POG091H03XW; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:UniProtKB-UniRule.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR009154; Membr-bd_4haem_cyt_TorC.
DR   InterPro; IPR011031; Multihaem_cyt.
DR   InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR   Pfam; PF03264; Cytochrom_NNT; 1.
DR   PIRSF; PIRSF000014; 4_hem_cytch_TorC; 1.
DR   SUPFAM; SSF48695; SSF48695; 1.
DR   TIGRFAMs; TIGR02162; torC; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 2.
PE   3: Inferred from homology;
DR   PRODOM; C5BCT6.
DR   SWISS-2DPAGE; C5BCT6.
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR000014};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR000014};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000014};
KW   Heme {ECO:0000256|PIRNR:PIRNR000014, ECO:0000256|PIRSR:PIRSR000014-1};
KW   Iron {ECO:0000256|PIRNR:PIRNR000014, ECO:0000256|PIRSR:PIRSR000014-2};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000014};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transport {ECO:0000256|PIRNR:PIRNR000014}.
FT   DOMAIN       43    179       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51008}.
FT   DOMAIN      324    338       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51008}.
FT   METAL        52     52       Iron (heme 1 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000014-2}.
FT   METAL        81     81       Iron (heme 2 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000014-2}.
FT   METAL       142    142       Iron (heme 3 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000014-2}.
FT   METAL       174    174       Iron (heme 4 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000014-2}.
FT   METAL       333    333       Iron (heme 5 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000014-2}.
FT   BINDING      48     48       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING      51     51       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING      77     77       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING      80     80       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING     138    138       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING     141    141       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING     170    170       Heme 4 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING     173    173       Heme 4 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING     329    329       Heme 5 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
FT   BINDING     332    332       Heme 5 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000014-1}.
SQ   SEQUENCE   391 AA;  43805 MW;  3B03386DE0291B39 CRC64;
     MKKLWNRLNR PSTRWSVLAL LALGIVIGLA LIVLPHVGIK MTSTTEFCVS CHSMQPVYQE
     YKQSVHFKNA SGVRAECHDC HIPPDIPGMV KRKLEASNDI YQTFIAHSID TPEKFEAKRA
     ELAEREWKRM KENNSATCRS CHNYDAMDHA KQHPEAARQM AIAAKDNQSC IDCHKGIAHQ
     LPDMSSGFRK QFAELRQNAS DEGNTLYTLD MKPIYAAKGD KEPAGSLLPA SEITVQKRDG
     DWLQVQIEGW TETNGRQRVL SLLPGKRIFV SSIRDQVQQN AKTLEKTTVA ATGVEWSKLQ
     ATAWVQKGDL VNNIKPIWAY ADALYNGTCN QCHGAPEKAH FDANGWIGTL NGMIGFTSLD
     KREERTLLKY LQMNASDTGG AAQKHEGRET R
//

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