CYCC_GEOSL
ID CYCC_GEOSL Reviewed; 768 AA.
AC Q749L1; Q93M26;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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; Synonyms=ferA; OrderedLocusNames=GSU2731;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-459, PROTEIN SEQUENCE OF 275-281 AND
RP 341-348, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=11563978; DOI=10.1042/0264-6021:3590147;
RA Magnuson T.S., Isoyama N., Hodges-Myerson A.L., Davidson G., Maroney M.J.,
RA Geesey G.G., Lovley D.R.;
RT "Isolation, characterization and gene sequence analysis of a membrane-
RT associated 89 kDa Fe(III) reducing cytochrome c from Geobacter
RT sulfurreducens.";
RL Biochem. J. 359:147-152(2001).
RN [3]
RP FUNCTION.
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).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=15345398; DOI=10.1128/aem.70.9.5183-5189.2004;
RA Chin K.J., Esteve-Nunez A., Leang C., Lovley D.R.;
RT "Direct correlation between rates of anaerobic respiration and levels of
RT mRNA for key respiratory genes in Geobacter sulfurreducens.";
RL Appl. Environ. Microbiol. 70:5183-5189(2004).
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:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Not regulated by Fe(3+). {ECO:0000269|PubMed:15345398}.
CC -!- PTM: Binds 12 heme c groups per subunit. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to act as an electron-transport mediator
CC in the dissimilatory reduction of Fe(3+).
CC {ECO:0000305|PubMed:11563978}.
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DR EMBL; AE017180; AAR36103.1; -; Genomic_DNA.
DR EMBL; AY033095; AAK53456.2; -; Genomic_DNA.
DR RefSeq; NP_953776.1; NC_002939.5.
DR RefSeq; WP_010943365.1; NC_002939.5.
DR AlphaFoldDB; Q749L1; -.
DR STRING; 243231.GSU2731; -.
DR TCDB; 5.B.3.1.1; the geobacter nanowire electron transfer (g-net) family.
DR EnsemblBacteria; AAR36103; AAR36103; GSU2731.
DR KEGG; gsu:GSU2731; -.
DR PATRIC; fig|243231.5.peg.2757; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_355545_0_0_7; -.
DR OMA; HYNWDDT; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IDA:TIGR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:TIGR.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Direct protein sequencing; Electron transport; Heme;
KW Iron; Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..768
FT /note="C-type polyheme cytochrome OmcC"
FT /id="PRO_0000429037"
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:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 768 AA; 80591 MW; 3253D240CC93E1A1 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 AIDAQVTAAR LDSATATAAK AYLGATRP
