ID I6Z8J7_MELRP Unreviewed; 1011 AA.
AC I6Z8J7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=PAS:Response regulator receiver:ATP-binding region, ATPase-like:Histidine kinase A-like protein {ECO:0000313|EMBL:AFN75480.1};
GN OrderedLocusNames=MROS_2250 {ECO:0000313|EMBL:AFN75480.1};
OS Melioribacter roseus (strain JCM 17771 / P3M-2).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Melioribacteraceae; Melioribacter.
OX NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN75480.1, ECO:0000313|Proteomes:UP000009011};
RN [1] {ECO:0000313|EMBL:AFN75480.1, ECO:0000313|Proteomes:UP000009011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT organotrophic bacterium representing a novel deep lineage within
RT Bacteriodetes/Chlorobi group.";
RL PLoS ONE 8:E53047-E53047(2013).
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DR EMBL; CP003557; AFN75480.1; -; Genomic_DNA.
DR AlphaFoldDB; I6Z8J7; -.
DR STRING; 1191523.MROS_2250; -.
DR KEGG; mro:MROS_2250; -.
DR PATRIC; fig|1191523.3.peg.2376; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_277691_0_0_10; -.
DR Proteomes; UP000009011; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:AFN75480.1};
KW Kinase {ECO:0000313|EMBL:AFN75480.1};
KW Nucleotide-binding {ECO:0000313|EMBL:AFN75480.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000009011};
KW Transferase {ECO:0000313|EMBL:AFN75480.1}.
FT DOMAIN 372..443
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 488..558
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 625..828
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 892..1008
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 940
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1011 AA; 115968 MW; B1BE7F8C1AAF11FC CRC64;
MNYENKHGLI VDKNGKIIAV SNDIKKLFPG LSPQNNFLQY WKDVQSVDKE YKFRIIEKFE
ECRRNNAPAA FDLPLTINDN RLTYTLVYTP LKSENNIYFY IDFILSGKSK TEETDTYKIR
IALNQIEDLI EDDEILKVID RVKNSYPFTF IEKVKFQKEI NGLKNFFWIK DRDDKIVVAN
EAYASWLGTT PSKLENKSES DYLPKYLVNL YSRLNEYIKN TSNIIAVSGL KSAGDTKNFS
IYLLPVCDLE NNVIALIGFS YVETDKEIVR SLTRHIPLPA CVVGENLELT EYNEKFESVF
ELSGKKSKLH EVFGRDAVNK IASFLKENKK YEDKLFDIET ADKKLYSFTA LKEVDRVILS
GYHVEKQTDE NASLDIEDYL KIVPDAAYVY DLENLKFLAV TDEALKLYGY SKEKFLELDL
TDLYAPEDVQ ALIQSDDKSL RGKPLKHKRS DGKDIYVTIK SVEISYKGKK AHLNLVREVS
FELKTRRENQ LYRHVFENTG DLVIVTDKDG FIVSINDSVT RQLGFSQREL EGRPIISIVS
DEDRAVVNKN VLHAESNNTI KLNVSVKKSE GELTEAEIAA SKIKDYEGKV EQVVFLIRLQ
PEEKRNLTAE VANETSNIDA AFLSNLFHEL LTPLNVIMGF TQDLWENIEN PNDEQKESVE
IIKENQRTLL QIMDNAVEYA AFLRKNIKYK IENVRLTDLL PELEEVITKT AKQHGKTVKE
GKISSSLEFE TDKQKFLSLL GMLINFAVTI TKEKELKLSA KKEDDDNLII LIDDLKEGAS
PYLLKGMHDI LTDDENLNRR NYGFSRFSMK LAKKLMEILG ISFKTLGDKD KKRVGIVVPF
KFTPFEGGEI EIEESPRPVE EKFERPAEKP ISNVVEKQAT NMLKKLDLTS MTCLYLEDQV
DSQILFKSQM KDLKTIEVAP SLEAAIPLLK TRRFDFLIVD INLQGEYNGL DVLRIVRKMP
GYKDIPIIAS TAYMQPGARE NFIAAGFTDF ISKPLLRDKV IEILTRIYSA S
//
