ID A0A0X8D8Q7_9BACL Unreviewed; 688 AA.
AC A0A0X8D8Q7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Fis family transcriptional regulator {ECO:0000313|EMBL:AMA72950.1};
GN ORFNames=ACH33_08810 {ECO:0000313|EMBL:AMA72950.1};
OS Aneurinibacillus sp. XH2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA72950.1, ECO:0000313|Proteomes:UP000065566};
RN [1] {ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA Xi L.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMA72950.1, ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA72950.1,
RC ECO:0000313|Proteomes:UP000065566};
RA Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT China.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP014140; AMA72950.1; -; Genomic_DNA.
DR RefSeq; WP_057898685.1; NZ_CP014140.1.
DR AlphaFoldDB; A0A0X8D8Q7; -.
DR STRING; 1450761.ACH33_08810; -.
DR KEGG; anx:ACH33_08810; -.
DR Proteomes; UP000065566; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR030828; HTH_TypR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR PANTHER; PTHR32071:SF57; SIGMA L-DEPENDENT TRANSCRIPTIONAL REGULATOR YQIR-RELATED; 1.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF18024; HTH_50; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000065566};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..63
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 117..163
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 303..354
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 379..608
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT COILED 345..372
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 688 AA; 78943 MW; DD4D1235799997E0 CRC64;
MITWKQILRP ISAVVNREST IQDVLREMHE RGADIAFVMD KGNIVGFIHT DSLLEQLRHT
PDLQQPIQYR KDILKVPYMH PVEYYHNISV VLGVNPGGEI IGYSLVQQAR HQMNELQLRH
MNQILDGAGV GIIRTNTRFE IEFINETAEN ILGLSRSFLL SRNYKTLLTM DKDLDRVIQG
ETFISVNSSI NFKQISGNFS PLRIDGRITG LVHVFFLREA FEEAVQELEF VRNLYSDLQA
VYSSSHEQIL VVNPKGEVIR LAGTFLQEFW GLDQPEKVIG RNVAEFERKG VFRPNIVDLC
IKKKKKLTMI QDTVHGRKVW SVATPVYHEG KLEKVVVLSR DITKTNQLQE ELKRVTKKSN
TYKQELDQLM NRYSADKPLI YRSRIMEDLV EEVKRIAQVD STVLLEGESG VGKEVFARTL
HAASRRKDYP LIRVNCGAIP ENLIESELFG YEKGAFTGAD QKGKPGLFEM AHRGTIFLDE
ISELSLNMQV KLLRVLQEKE VTRIGGVQTI PVDVRVIAAT NKNIKDMMEQ GEFREDLYYR
LNVIPIHIPP LRERTEDIFS LVLYFSQQFN RTYQMEKGFS PGALEVLENY DWPGNVRELQ
NIVERLIVTS REEFIQREDV LRVLYGEAGG KRKKTMVFEL MPLKEAVAEL ESQLIQLGLK
KYGTAAKVSE VLGVSPATIS RRMNKLFK
//
