ID A0A941LDL3_9BACT Unreviewed; 358 AA. AC A0A941LDL3; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 24-JAN-2024, entry version 5. DE SubName: Full=C-type cytochrome {ECO:0000313|EMBL:MBS0158669.1}; GN ORFNames=JSS26_08780 {ECO:0000313|EMBL:MBS0158669.1}; OS Nitrospira sp. OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae; OC Nitrospira. OX NCBI_TaxID=70125 {ECO:0000313|EMBL:MBS0158669.1, ECO:0000313|Proteomes:UP000738201}; RN [1] {ECO:0000313|EMBL:MBS0158669.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AMP-bin2 {ECO:0000313|EMBL:MBS0158669.1}; RX PubMed=33819658; RA Wang Y., Zhao R., Liu L., Li B., Zhang T.; RT "Selective enrichment of comammox from activated sludge using RT antibiotics."; RL Water Res. 197:0-0(2021). RN [2] {ECO:0000313|EMBL:MBS0158669.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AMP-bin2 {ECO:0000313|EMBL:MBS0158669.1}; RA Wang Y., Cao Y., Meng X., Hu T., Wang S., Cao K.; RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR000294-1}; CC Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}. CC -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294- CC 1}. 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:MBS0158669.1}. 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; JAFEBF010000008; MBS0158669.1; -; Genomic_DNA. DR Proteomes; UP000738201; Unassembled WGS sequence. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. 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 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 InterPro; IPR026259; MauG/Cytc_peroxidase. DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1. DR PANTHER; PTHR30600:SF10; METHYLAMINE UTILIZATION PROTEIN; 1. DR Pfam; PF03150; CCP_MauG; 1. DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1. DR SUPFAM; SSF46626; Cytochrome c; 2. DR PROSITE; PS51007; CYTC; 1. PE 4: Predicted; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000294-2}; KW Periplasm {ECO:0000256|ARBA:ARBA00022764}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..358 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5037797099" FT DOMAIN 220..343 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT BINDING 89 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 92 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 93 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:0000256|PIRSR:PIRSR000294-2" FT BINDING 235 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 238 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 239 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:0000256|PIRSR:PIRSR000294-2" SQ SEQUENCE 358 AA; 39258 MW; E9DF1D817EB9A230 CRC64; MGMRRMRWVA GMAASIMVGA MGMAATNVLG DSSAPSPGGS STTTQAVPLG LEDPAAYIPT DNPQTAKKIE LGRILFFDKR LSKTNTVACA NCHMPGLAFT DGQAVSMGIN RLQGGRSAPT AINRVYSKMQ FWDGRAQTLE EQSTGPFVNP VEHGFLDYDE MTAKMKQISG YRKLFEEVFH DEITEKNIGK AIASFQRTLI SGNSPADRFD VGGEEQALTD SAKRGLELFR GKARCTRCHS GFNFSDEKFH NLGIGWDTNS VDLGRYMVTK NPEDIGAFKT PTLREIARTA PYMHDGRFGT LEDVVKFYNQ GGISNPHQDN TIIPLELSNG EQQDVVAFLR SLNGEGWQQV AAPIEFPQ //