CYCB_GEOSL
ID CYCB_GEOSL Reviewed; 744 AA.
AC Q749K5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=C-type polyheme cytochrome OmcB;
DE AltName: Full=Outer membrane c-type cytochrome B;
DE Flags: Precursor;
GN Name=omcB; OrderedLocusNames=GSU2737;
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.
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 [3]
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: Involved in anaerobic respiration with Fe(3+) as terminal
CC electron acceptor. Acts as an electron-transport mediator in the
CC dissimilatory reduction of Fe(3+). {ECO:0000269|PubMed:12644478}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by Fe(3+). {ECO:0000269|PubMed:15345398}.
CC -!- PTM: Binds 12 heme c groups per subunit. {ECO:0000305}.
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DR EMBL; AE017180; AAR36109.1; -; Genomic_DNA.
DR RefSeq; NP_953782.1; NC_002939.5.
DR RefSeq; WP_010943369.1; NC_002939.5.
DR AlphaFoldDB; Q749K5; -.
DR STRING; 243231.GSU2737; -.
DR TCDB; 5.B.8.1.1; the trans-outer membrane electron transfer porin/cytochrome complex (et-pcc) family.
DR EnsemblBacteria; AAR36109; AAR36109; GSU2737.
DR KEGG; gsu:GSU2737; -.
DR PATRIC; fig|243231.5.peg.2761; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_355545_0_0_7; -.
DR OMA; TCKACHT; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; 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 InterPro; IPR012286; Tetrahaem_cytochrome.
DR Pfam; PF14537; Cytochrom_c3_2; 1.
DR SUPFAM; SSF48695; SSF48695; 2.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 2: Evidence at transcript level;
KW Cell outer membrane; Electron transport; Heme; Iron; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..744
FT /note="C-type polyheme cytochrome OmcB"
FT /id="PRO_0000429039"
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 81
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 /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 85
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 107
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 110
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 111
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 141
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 144
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 145
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 185
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 188
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 189
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 225
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 228
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 229
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 303
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 306
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 307
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 382
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 385
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 386
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 430
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 433
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 434
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 480
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 483
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 484
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 555
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 558
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 559
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 587
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 590
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 591
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 744 AA; 77177 MW; 7BC25F00F986DF9D CRC64;
MSRKVTKYSA VLAVSLFAAA LAGCGSENKE GTVGTGPGGV ATVGDSACVQ CHSAVTEALT
GESLIAQYQK SSPHNTAGLG CESCHGGGAQ HNGVGPIPFA QPDASRCADC HDGTTAVATN
SDTAFAESRH NIQTIRSGAT CRRCHTHEGA VLSNIAGYTG DLATLEDTVN QNKVPLVSSY
SQISCATCHE HGGGLRTIKA TNGAAGPVVN WDPNNNRTVD QFDLCTSCHN MYSYNGSTLL
TNGVPVNGVA TGTVGHHETT WYRIIATTHF DNYSTGPQAG AGASGTNAKV EGYVLRRTGA
NPCFDCHGHE AKTNTRPGRD ATIHTDWAKS AHAGGLLTAK YNAVGALTGA AAVNAAMNAY
VDDTTAIAWT HYNWDASSRG SCQRCHTATG AANFMSNPAG YDPTGAGNSF SHLQGWSAAN
GSKQNELLYC WGCHTNAGTG ELRNPGAITE NYAGVNSTST GTTGTAVTIS YPDIAGSNVC
MTCHLGREAG ENIKAITDAD GILGFVNSHY LAAGGQLFGK TGYEYATRSY AKPTFFAHDK
IGTAAAPGTG TNGPCAGCHM TTPNSHSFLP VTKDGTGAVT AITSTACATC HAGAYALTPE
ALTAEEEEYV ASLEALKAAL AGKGILFFNA HPYFYRDTNA NGIGDPGELV SSNAFTNWAG
VYGLALWKDV MGAAFNANLL IHDPGGYAHN RFYVKRLIWD SIDFIYDGVL NNDVTAAIDA
QVTATRLDSA TATAAKAYLG TTRP
