CYCC_GEOSK
ID CYCC_GEOSK Reviewed; 768 AA.
AC D7ALP6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=C-type polyheme cytochrome OmcC;
DE AltName: Full=Outer membrane c-type cytochrome C;
DE AltName: Full=Polyheme membrane-associated cytochrome c;
DE Flags: Precursor;
GN Name=omcC; OrderedLocusNames=KN400_2673;
OS Geobacter sulfurreducens (strain DL-1 / KN400).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=663917;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-1 / KN400;
RX PubMed=20544019; DOI=10.1371/journal.pone.0010922;
RA Nagarajan H., Butler J.E., Klimes A., Qiu Y., Zengler K., Ward J.,
RA Young N.D., Methe B.A., Palsson B.O., Lovley D.R., Barrett C.L.;
RT "De Novo assembly of the complete genome of an enhanced electricity-
RT producing variant of Geobacter sulfurreducens using only short reads.";
RL PLoS ONE 5:E10922-E10922(2010).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=DL-1 / KN400;
RX PubMed=12644478; DOI=10.1128/jb.185.7.2096-2103.2003;
RA Leang C., Coppi M.V., Lovley D.R.;
RT "OmcB, a c-type polyheme cytochrome, involved in Fe(III) reduction in
RT Geobacter sulfurreducens.";
RL J. Bacteriol. 185:2096-2103(2003).
CC -!- FUNCTION: Not involved in Fe(3+) reduction.
CC {ECO:0000269|PubMed:12644478}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- PTM: Binds 12 heme c groups per subunit. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No impact on growth with fumarate, or on the
CC ability to reduce Fe(3+). {ECO:0000269|PubMed:12644478}.
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DR EMBL; CP002031; ADI85485.1; -; Genomic_DNA.
DR RefSeq; WP_014551954.1; NC_017454.1.
DR AlphaFoldDB; D7ALP6; -.
DR KEGG; gsk:KN400_2673; -.
DR PATRIC; fig|663917.3.peg.2679; -.
DR HOGENOM; CLU_355545_0_0_7; -.
DR OMA; HYNWDDT; -.
DR OrthoDB; 738283at2; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR023155; Cyt_c-552/4.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF13435; Cytochrome_C554; 1.
DR SUPFAM; SSF48695; SSF48695; 2.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Electron transport; Heme; Iron; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..768
FT /note="C-type polyheme cytochrome OmcC"
FT /id="PRO_0000429038"
FT BINDING 48
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 52
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 80
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 84
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 112
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 148
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 151
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 152
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 193
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 196
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 197
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 238
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 241
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 242
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 320
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 323
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 324
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 405
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 408
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 409
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 454
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 457
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 458
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 504
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 507
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 508
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 579
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 582
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 583
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 611
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 614
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 615
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 768 AA; 80651 MW; 3253D247BD23E1A1 CRC64;
MSRKVTKYSA VLAVSLFAAA LAGCGSENKE GTVGTGPGGV ATVGDTACVQ CHSAVVDPLT
GESIITQYTR SFHYSKGVGC EGCHGGGAQH NGVGPLPFPL AGQSEAQIAA RCASCHNGVI
APLSSSPNFV NGNHANPFGG EEAKENLCSR CHSHEGAIFG AQAGFTGDGN ILRNAAYQPV
YPQDPETFNV MTCATCHQHG GAQRQVFTQI STAGVPNSRR TVAWDPNRNS INDQYDLCTS
CHTVNTMTGT LIGSGNVLQI FTSNAVGSGT KSVTTAPFYH NTRWFRTLPS THYDFPESKT
TASGTTIEGY VIRRNTANPC FDCHGHEFQT NTRRLAGADR PNTIFLDWGQ SAHGGKLLQA
KVAAAALASS GAAEVDDVMK AGATDATAPG WTHYNWDDTA SRGACQRCHT STGASNFLNN
PAGYDRTGAG NSFTHLAGWT SSNKRSDQNE LLYCWGCHTK AGTGELRNPG AITEVYPGIN
STSTGTTGLD VTVSYPDIKG SNVCMGCHLG REVGDNIKAI TDADGILGFV NSHYLTAGGQ
LFGTTGYEYA TRSYANPAFF QHDKIGTAAA PGTGTNGPCA GCHMTTPTSH LFLPVTKDGT
GAITAITSTA CVTCHAGTFA LTPEGLTAEE EEYVASLEAL KAALAGKGIL FFNAHPYFYR
DTNANGIADP GETVSSNAFT NWAGVYGLAL WQDVMGAAFN ANLLIHDPGG YAHNRFYSKR
LIWDSIDFIF DGVLNNDVTA AIDAQVTATR LDSATATAAK AYLGTTRP
