ID A0A1F8KHM9_9CHLR Unreviewed; 309 AA.
AC A0A1F8KHM9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Cytochrome b561 bacterial/Ni-hydrogenase domain-containing protein {ECO:0000259|Pfam:PF01292};
GN ORFNames=A2X25_03665 {ECO:0000313|EMBL:OGN73842.1};
OS Chloroflexi bacterium GWB2_49_20.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN73842.1};
RN [1] {ECO:0000313|EMBL:OGN73842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN73842.1}.
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DR EMBL; MGMF01000017; OGN73842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8KHM9; -.
DR STRING; 1797612.A2X25_03665; -.
DR Proteomes; UP000178842; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.950.20; Transmembrane di-heme cytochromes, Chain C; 1.
DR InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR PANTHER; PTHR30485; NI/FE-HYDROGENASE 1 B-TYPE CYTOCHROME SUBUNIT; 1.
DR PANTHER; PTHR30485:SF0; NI_FE-HYDROGENASE 1 B-TYPE CYTOCHROME SUBUNIT-RELATED; 1.
DR Pfam; PF01292; Ni_hydr_CYTB; 1.
DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..239
FT /note="Cytochrome b561 bacterial/Ni-hydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01292"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 34910 MW; 01728D993C6CC3F7 CRC64;
MENNPVQESA AMPETVEPVN ETTSRMPTIT RYVNERDANA ALQNMKTSKD GSAYVVRFTL
LVRLLHLLLL VAVTGLAFTG LAQIFYANAL GRIMLSLLGG LEKTQNIHHA FAILLAALAI
FHILDSLESL FVRQQRPPML LRWIDFQNFF QMQVFNLGLT RKQPRFDRYS YEEKAVYWLV
TLGILVLGLT GIVQWFPIQV TEFLPGIVIP YAGIIHRWEA ILVILVVFVY HLYQVLFRKP
DGSIFSGKKT RADMQMEHPL ELEYLEKAAA AAGSPDWPVR IELNLSDDTG EEIKETESAS
RDTSAPEGS
//
