ID A0A259UBH8_9FIRM Unreviewed; 972 AA.
AC A0A259UBH8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=barA_3 {ECO:0000313|EMBL:OZC15449.1};
GN ORFNames=SPSIL_41500 {ECO:0000313|EMBL:OZC15449.1};
OS Sporomusa silvacetica DSM 10669.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1123289 {ECO:0000313|EMBL:OZC15449.1, ECO:0000313|Proteomes:UP000216752};
RN [1] {ECO:0000313|EMBL:OZC15449.1, ECO:0000313|Proteomes:UP000216752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10669 {ECO:0000313|EMBL:OZC15449.1,
RC ECO:0000313|Proteomes:UP000216752};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa silvacetica DSM 10669.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:OZC15449.1}.
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DR EMBL; LSLK01000100; OZC15449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259UBH8; -.
DR OrthoDB; 9805486at2; -.
DR Proteomes; UP000216752; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:OZC15449.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000216752};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:OZC15449.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 271..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..551
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 572..695
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 722..838
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 878..972
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 627
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 773
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 917
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 972 AA; 110370 MW; 9DFEB138C9B4114F CRC64;
MKLLRNIFLS IVVLPFFITI CFAAQKDIQF TQMERDFIKE HPVIHLGVDP KFIPYEFIDT
DGVYKGIAAD YIKLISERTG LEFVVEKNLS WPEAYEKGVL KLLDALPCVS KTKEREQYFL
YSEPYYSFQR VIYINENNNT IKNFADVMNR KVAVQTNSSH HSYLKAFESI KPSPYFNVAE
ALRAVSDGRE EAFIGNLATS NYLIKANGIT NLKYVKVASE EKQSLYFAVR QDWPILVSIL
NKALADITQE EKINIDNRWL GVENRIDYTQ IIRIVGIAGA VITIILLVSL YWIVKLRREV
ETRKRIEEAL KVAKEEAEYA NHVKSTFLAR MSHEIRTPLN AITGMAYVIK KTDVTTIQKV
YLDKITRAAR DMLGIINDIL DFSKIEAGKI DIERTSFNLD DILEQLISIV SFKIDEQNID
FSMNRDPEIP TFFWGDQKRI QQVLLNIVNN AVKFTKDGAV SLTIRLVAKV KDSYIIEFSV
KDTGIGMSNE QLEQLFAPFS QGDSSISRRF GGTGLGLSIV KSLVEQMGGS IEVYSAVDEG
STFNIQLTLE ADRNKDYEEK KKAASVYFQN IRVLVVEKNA FYRNLLSGYL NSFNMVAEFA
TSEARAMELM EKVSREAGTS YNLLIVDYET PQDGGIAFCT KVKRLPWLKE IPKFIVMIPL
SKEEFFKNLE DAGLDFGITK PIIPSILYNG IVEIFKINVI EMHESSALIT TQNPFMVEYP
YHVLIVEDNK TNQFIAQSIL EQSGFRVTLA DDGVEGYELF LKMQKDLDLV LMDIHMPVMS
GYEATSLIRN VDSNIPIIAM TADAIAGVEE KCKSIGIDHY ISKPFDPEQF VETIWQVVKP
YKEGLLIKSG GEAKPEDPIK LNEGVLDEKD GIRHMGGNVD LYEMVLKEYY NENLETSLIL
NRTIEKENYE EAAQIVHKIK SSSGSIGAKG LHEAASNLQR SLSNGEVEII PKLHKEFDEI
LKQLLSVIAL RK
//
