ID A0A258WQL0_9SPHI Unreviewed; 1127 AA.
AC A0A258WQL0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Crp/Fnr family transcriptional regulator {ECO:0000313|EMBL:OYZ30461.1};
GN ORFNames=B7Y24_13225 {ECO:0000313|EMBL:OYZ30461.1};
OS Sphingobacteriales bacterium 16-39-50.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1970581 {ECO:0000313|EMBL:OYZ30461.1, ECO:0000313|Proteomes:UP000216983};
RN [1] {ECO:0000313|EMBL:OYZ30461.1, ECO:0000313|Proteomes:UP000216983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-39-50 {ECO:0000313|EMBL:OYZ30461.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602324-1}.
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:OYZ30461.1}.
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; NCHA01000017; OYZ30461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258WQL0; -.
DR Proteomes; UP000216983; 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:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002324; Cyt_c_ID.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR029010; ThuA-like.
DR PANTHER; PTHR40469:SF2; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF00801; PKD; 1.
DR Pfam; PF06283; ThuA; 1.
DR PRINTS; PR00606; CYTCHROMECID.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602324-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602324-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602324-1}.
FT DOMAIN 732..793
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 848..943
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 872
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
FT BINDING 876
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
FT BINDING 921
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
SQ SEQUENCE 1127 AA; 125141 MW; 45FFE35EE978B4DD CRC64;
MKRIYKLLPF SLLILALFAF TKWEQAVKPR VLVFSKTAAY RHESIAAGKT ALIKLGMENG
FIVDTTENEN YFNDDSLKNY SAVIFLSTTG NILNSPQQIS FERFIQAGGS YVGIHAAADT
EYDWEWYGKL VGGYFISHPK IQDATMIVND RTHLSTKHLD EKWVHKDEWY NYKNLNRNVK
VLISLDEKSY TGGENGDYHP IAWHHEFDGG RAFYTGMGHT NEAYSDQLFL KHLLGGIKYA
IGNNVPLNYA KAKTPPVPEE NRFVKTVLTT GTLFEPTEMA ILPNLDILLV QRRGEIMLYK
EKSKSISQVG FLNAYHKTAV AGVNAEEGVL GIATDPAFKD NNYVYIFYSP IDTSVNRLSR
FKFVDDKLDN SSEKVILEFY SQREICCHTG GSIAFGPDGL LYVSAGDNAT PFDVPKQAFV
NKGYGPMDNR PGLEQYDARR SSGNTNDLRG KIMRIKVNED GSYSIPEGNL FPPNTPGTRP
EIYVMGNRNP YRISIDKKTG FLYWGEVGPD ANADSPERGS RGYDELNQAR KAGFFGWPFF
VGNNYPYRAY DYTNGTAGEA FDPAKPYNNS PNNTGLEYLP PVSPAFIWYP YAASKEFPQV
GTGGRNAMAG PVYHPELYPK ETRYPDYYAN KLFIYDWIRG WIKAVTMKPN GDYDNMEAFM
PMTNFSSPID MELGPDGRIY ILEYGKGWFS KNPDAAISRI DFVAGNRPPK IKELIISKTS
GVLPFKLQAK VEASDPDKDK MNYVWELGSG IKKSTVMPNI EHTFTKAGEY AISVLAIDKN
FASTNSSPIT ISAGNAQPKV SIKLKGNQSF YFAGKPVEYD VSVSDEGATV NKNTIYVANN
YTKGTDLAGA SMGHQVFTEA QAGQALMLKS DCQSCHQVST KSIGPSYTQV SAKYQNDPNA
VSYLSAKIIK GGGGTWGEVA MPAHSAMSDD DAKKIAQWVL SLEDKAVNKA TLPIQGSIIP
AQESENNIFS IYASYTDQGQ AGLKPLTGSA TVYLRSNIFN AREITERTRI GLKDSTNTGF
LIYPQNNGWF KLSNLDLSGI RNLELANLSK GGGGIYDIEI RANSESGALL GKGNFKDGEV
IDQQSNTLIQ LNLPADMRIN SMFVLFVSDP KNLKPRPLLK TVTFKPE
//
