ID   A0A941LDL3_9BACT        Unreviewed;       358 AA.
AC   A0A941LDL3;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   27-MAR-2024, entry version 6.
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}.
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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|ARBA:ARBA00022729, 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
//