ID A0A0J9E859_9RHOB Unreviewed; 370 AA.
AC A0A0J9E859;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Carbon monoxide dehydrogenase operon C protein {ECO:0000313|EMBL:KMW57949.1};
GN ORFNames=AIOL_002917 {ECO:0000313|EMBL:KMW57949.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW57949.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW57949.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW57949.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMW57949.1}.
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DR EMBL; LFTY01000002; KMW57949.1; -; Genomic_DNA.
DR RefSeq; WP_049643614.1; NZ_LFTY01000002.1.
DR AlphaFoldDB; A0A0J9E859; -.
DR STRING; 1675527.AIOL_002917; -.
DR PATRIC; fig|1675527.3.peg.3054; -.
DR OrthoDB; 9781059at2; -.
DR Proteomes; UP000037178; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR Gene3D; 2.40.50.1020; LytTr DNA-binding domain; 1.
DR InterPro; IPR007492; LytTR_DNA-bd_dom.
DR InterPro; IPR012073; LytTR_MHYT.
DR InterPro; IPR005330; MHYT_dom.
DR PANTHER; PTHR35152; -; 1.
DR PANTHER; PTHR35152:SF1; DOMAIN SIGNALLING PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G11310)-RELATED; 1.
DR Pfam; PF04397; LytTR; 1.
DR Pfam; PF03707; MHYT; 2.
DR PIRSF; PIRSF036615; MHYT_LytTR; 2.
DR SMART; SM00850; LytTR; 1.
DR PROSITE; PS50930; HTH_LYTTR; 1.
DR PROSITE; PS50924; MHYT; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Reference proteome {ECO:0000313|Proteomes:UP000037178};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 44..68
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 74..101
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 108..131
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 8..195
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 265..370
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
SQ SEQUENCE 370 AA; 38964 MW; 5C93305CDD3527F8 CRC64;
MDFLEFSHNP GLVAASVIVA LLAGFTGLNL TKDLSSKSVR QRKMAVALAS VALGGGIWSM
HFVAMLGLQL PILFYYDAAI TLASALVCIL IVGVALILLH FTERTRATIV AAGALVGAGI
LAMHYIGMAG LELCRAVYTP SGLISAGVLA MGLCVAAFGV AYGQRSDRNI LLGTLCFGLA
VAAVHFAAVA GTRFVKVPGF TEFGPIMSNE VLALGVILSS FVLFGAFLWV GVTYLMPRPA
TGPAAGAEAA ADPPLAAPAT PPMRIPCERD GGKLFIAAAD VAFVRADGHY TQVYTDGERL
FCVWPITEAT KRLLPQGFLK VHRSYLINPA KVAAFERKKD SGRCTFEADD LPHVPVSRSN
LKDVQLALGA
//
