ID L7CDD3_RHOBT Unreviewed; 424 AA.
AC L7CDD3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Di-heme cytochrome c peroxidase {ECO:0000313|EMBL:ELP31983.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:ELP31983.1};
GN ORFNames=RBSWK_04138 {ECO:0000313|EMBL:ELP31983.1};
OS Rhodopirellula baltica SWK14.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=993516 {ECO:0000313|EMBL:ELP31983.1, ECO:0000313|Proteomes:UP000010959};
RN [1] {ECO:0000313|EMBL:ELP31983.1, ECO:0000313|Proteomes:UP000010959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWK14 {ECO:0000313|EMBL:ELP31983.1,
RC ECO:0000313|Proteomes:UP000010959};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELP31983.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMWG01000117; ELP31983.1; -; Genomic_DNA.
DR RefSeq; WP_007338925.1; NZ_AMWG01000117.1.
DR AlphaFoldDB; L7CDD3; -.
DR PATRIC; fig|993516.3.peg.4425; -.
DR Proteomes; UP000010959; Unassembled WGS sequence.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR PANTHER; PTHR30600:SF10; METHYLAMINE UTILIZATION PROTEIN; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:ELP31983.1};
KW Peroxidase {ECO:0000313|EMBL:ELP31983.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..424
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003972240"
FT DOMAIN 103..230
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 285..408
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 424 AA; 46291 MW; 389A1A6AD5610DB8 CRC64;
MLRFNDAFPN TLNFTMTIHR FLMCAAATLV AAGPTAFAAE TVSLGDPTLT AGIPGDGPLT
LEQAQRFLAD DDNHTELNVE LPKGLDAASG NIYIPEDNPI TRAKIELGRQ LYFDPRLSAD
GTISCATCHA PETGWGAPTQ FGEGIRGQTG NRNSPVSFNR ILSKHQFHDG RAASLEEQAV
GPIANPIEMG NTHEVCVKTL ADNPVYKAQF DKVFDDGVTI DNIGKALATF ERAIVTGPAP
YDYYAPLSAF EKTFAEDLEY LDEEPALAEQ YAKLKEEAAK NPMTESSIRG MELTFGKANC
TACHAGANFT DEQFHNIGVG MDSENPDLGR FEVTKEEKDR GAFKTPTMRN VADTGPYMHD
GSQATLEEVI EWYNKGGHPN PYLSDKMKPL NLTEQEKADL VEFMRQGLQS DFPVIEAGRL
PAEG
//