OMCS_GEOSL
ID OMCS_GEOSL Reviewed; 432 AA.
AC Q74A86;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=C-type cytochrome OmcS {ECO:0000303|PubMed:20400557};
DE AltName: Full=Outer membrane cytochrome S {ECO:0000303|PubMed:16332857};
DE Flags: Precursor;
GN Name=omcS {ECO:0000303|PubMed:16332857};
GN OrderedLocusNames=GSU2504 {ECO:0000312|EMBL:AAR35877.1};
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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DL1;
RX PubMed=16332857; DOI=10.1128/aem.71.12.8634-8641.2005;
RA Mehta T., Coppi M.V., Childers S.E., Lovley D.R.;
RT "Outer membrane c-type cytochromes required for Fe(III) and Mn(IV) oxide
RT reduction in Geobacter sulfurreducens.";
RL Appl. Environ. Microbiol. 71:8634-8641(2005).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20400557; DOI=10.1128/aem.00023-10;
RA Leang C., Qian X., Mester T., Lovley D.R.;
RT "Alignment of the c-type cytochrome OmcS along pili of Geobacter
RT sulfurreducens.";
RL Appl. Environ. Microbiol. 76:4080-4084(2010).
RN [4]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=GSU2215;
RX PubMed=21236241; DOI=10.1016/j.bbabio.2011.01.003;
RA Qian X., Mester T., Morgado L., Arakawa T., Sharma M.L., Inoue K.,
RA Joseph C., Salgueiro C.A., Maroney M.J., Lovley D.R.;
RT "Biochemical characterization of purified OmcS, a c-type cytochrome
RT required for insoluble Fe(III) reduction in Geobacter sulfurreducens.";
RL Biochim. Biophys. Acta 1807:404-412(2011).
RN [5]
RP FUNCTION IN DIET, AND INDUCTION.
RX PubMed=23377933; DOI=10.1128/aem.03837-12;
RA Shrestha P.M., Rotaru A.E., Summers Z.M., Shrestha M., Liu F., Lovley D.R.;
RT "Transcriptomic and genetic analysis of direct interspecies electron
RT transfer.";
RL Appl. Environ. Microbiol. 79:2397-2404(2013).
CC -!- FUNCTION: Plays an important role in extracellular electron transfer.
CC Can transfer electrons to insoluble Fe(3+) oxides as well as other
CC extracellular electron acceptors, including Mn(4+) oxide and humic
CC substances (PubMed:16332857, PubMed:20400557, PubMed:21236241).
CC Essential for direct interspecies electron transfer (DIET) in
CC cocultures with G. metallireducens (PubMed:23377933).
CC {ECO:0000269|PubMed:16332857, ECO:0000269|PubMed:20400557,
CC ECO:0000269|PubMed:21236241, ECO:0000269|PubMed:23377933}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:21236241};
CC Note=Binds 6 low-spin heme groups per subunit.
CC {ECO:0000269|PubMed:21236241};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:16332857,
CC ECO:0000269|PubMed:20400557, ECO:0000269|PubMed:21236241}. Cell surface
CC {ECO:0000269|PubMed:16332857, ECO:0000269|PubMed:20400557,
CC ECO:0000269|PubMed:21236241}. Note=Loosely associated with the cell
CC surface (PubMed:16332857, PubMed:21236241). Localizes along the pili
CC (PubMed:20400557). {ECO:0000269|PubMed:16332857,
CC ECO:0000269|PubMed:20400557, ECO:0000269|PubMed:21236241}.
CC -!- INDUCTION: Expressed in the presence of insoluble Fe(3+) oxide and
CC during growth with fumarate as the sole electron acceptor, but not
CC during growth on soluble Fe(3+) citrate (PubMed:16332857). Induced in
CC the cocultures with G. metallireducens (PubMed:23377933).
CC {ECO:0000269|PubMed:16332857, ECO:0000269|PubMed:23377933}.
CC -!- MASS SPECTROMETRY: Mass=47015; Method=Electrospray; Note=With six heme
CC groups.; Evidence={ECO:0000269|PubMed:21236241};
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene inhibits Fe(3+) oxide
CC reduction, but does not impact reduction of fumarate or Fe(3+) citrate.
CC Deletion negatively impacts the expression of omcT.
CC {ECO:0000269|PubMed:16332857}.
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DR EMBL; AE017180; AAR35877.1; -; Genomic_DNA.
DR RefSeq; NP_953550.1; NC_002939.5.
DR RefSeq; WP_010943141.1; NC_002939.5.
DR PDB; 6EF8; EM; 3.70 A; A/B/C/D/E/F/G=26-432.
DR PDB; 6NEF; EM; 3.42 A; A=26-432.
DR PDBsum; 6EF8; -.
DR PDBsum; 6NEF; -.
DR AlphaFoldDB; Q74A86; -.
DR SMR; Q74A86; -.
DR STRING; 243231.GSU2504; -.
DR TCDB; 5.B.3.1.1; the geobacter nanowire electron transfer (g-net) family.
DR EnsemblBacteria; AAR35877; AAR35877; GSU2504.
DR KEGG; gsu:GSU2504; -.
DR PATRIC; fig|243231.5.peg.2531; -.
DR eggNOG; ENOG5033TG0; Bacteria.
DR HOGENOM; CLU_627971_0_0_7; -.
DR OMA; QMTPGGD; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR SUPFAM; SSF48695; SSF48695; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..432
FT /note="C-type cytochrome OmcS"
FT /id="PRO_5004284875"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:6NEF"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6NEF"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:6NEF"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6NEF"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6NEF"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:6NEF"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:6NEF"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 402..408
FT /evidence="ECO:0007829|PDB:6NEF"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:6NEF"
SQ SEQUENCE 432 AA; 45389 MW; 7C94037250B9E5E8 CRC64;
MKKGMKVSLS VAAAALLMSA PAAFAFHSGG VAECEGCHTM HNSLGGAVMN SATAQFTTGP
MLLQGATQSS SCLNCHQHAG DTGPSSYHIS TAEADMPAGT APLQMTPGGD FGWVKKTYTW
NVRGLNTSEG ERKGHNIVAG DYNYVADTTL TTAPGGTYPA NQLHCSSCHD PHGKYRRFVD
GSIATTGLPI KNSGSYQNSN DPTAWGAVGA YRILGGTGYQ PKSLSGSYAF ANQVPAAVAP
STYNRTEATT QTRVAYGQGM SEWCANCHTD IHNSAYPTNL RHPAGNGAKF GATIAGLYNS
YKKSGDLTGT QASAYLSLAP FEEGTADYTV LKGHAKIDDT ALTGADATSN VNCLSCHRAH
ASGFDSMTRF NLAYEFTTIA DASGNSIYGT DPNTSSLQGR SVNEMTAAYY GRTADKFAPY
QRALCNKCHA KD
