ID A0A1S9PJI9_9SPHI Unreviewed; 1388 AA.
AC A0A1S9PJI9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BC343_22070 {ECO:0000313|EMBL:OOQ61131.1};
OS Mucilaginibacter pedocola.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1792845 {ECO:0000313|EMBL:OOQ61131.1, ECO:0000313|Proteomes:UP000189739};
RN [1] {ECO:0000313|EMBL:OOQ61131.1, ECO:0000313|Proteomes:UP000189739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBZ30 {ECO:0000313|EMBL:OOQ61131.1,
RC ECO:0000313|Proteomes:UP000189739};
RA Huang J., Tang J.;
RT "Genomic analysis of zinc-resistant bacterium Mucilaginibacter pedocola
RT TBZ30.";
RL Submitted (JUL-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 -!- 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:OOQ61131.1}.
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DR EMBL; MBTF01000003; OOQ61131.1; -; Genomic_DNA.
DR STRING; 1792845.BC343_22070; -.
DR Proteomes; UP000189739; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd17574; REC_OmpR; 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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF07494; Reg_prop; 7.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000189739};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 808..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 885..1106
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1126..1239
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1267..1382
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 851..878
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1176
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1316
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1388 AA; 156380 MW; C291FAF7EB5A70D0 CRC64;
MMYKYFILAL FVFFVRDGFA QNQSMKFEHL GKKEGLSQIN VGCIIQDSRG FIWVGTRDGL
SKYDGYGFTN YRHDPQDPGS ISSSMVSDII EDHEGNIWMA TIIGLNKLDR RTGTFTKYLH
NDKDPNSLSD NILNKLAVDD RGNLWVASQG GLDYFDTKAG KFTKHFKHNP KDDSSLANDK
VSFIYIGANK QLWVGTTGGG LDLFDAKKQE FRHYRHNATD PRSISGNDIS CIYEDGKGRL
WIGTLNDALN QLERNSQTFV RYPYRNGAPN TISSNTLYAL NSDENGNLWI GSENGGLCIL
NPETGNFYTY KHDDIDKNSL TGNSIYGIAK DRLGNMWLGA FAGGINLFKR STESFTHYRH
SSLENSLSND FVLALYEDPE RNVWVGTDGG GVNKFDYKNG KVTHYMQQPG KNSITGNFVL
TVNQDHENNF WFGTWADGIS VFNAKTGVFT NIKNQPGNPN SLPGNNIYAL THTKDNTTWI
GTYNDGLSHY DPKTKKFSNY KYDAADPHSL SSDRVYSLLE DSHGNLWVGT FDGGLNLYNR
NTNSFIRYRH KAGTNSISDD NVPDLYEGRN GSIWISTFTG LNLFDPITRH FTVFTKKDGL
PSDIVYAARE DDDGKIWVST NNGLSMFDPV KRTFKNYSVE DGLQEDEFKS HSAYKGASGK
LYFGGVNGFN AFSPGQILKP EGFSPLVITS FQVFNKKVAA AKNSNDPSPL KQDISDTKSI
TLNYKQSVIS LEFAALDFTS ADKKQYAYIL EGFDKEWNFV GTRHTATYTN LPAGTYTFKV
KYQNMVGLWS PVTPGLTIIT QPPFWLTWWF KTLVVLIVVG IVLGIFRLRV RTIKAQKAIL
ERQVEDRTQR LNEMSKGERI LREEAEKARE EAEKANRAKS IFLATMSHEI RTPMNGVMGM
ATLLANTPLN REQQEYTETI KTCGDSLLNV INDILDFSKI ESGNMELDEH DFDLRDCIEA
VLDIFAEKAA RTNLDLVYQV EHNVPAQIIA DSLRLRQVLI NLVGNAVKFT AKGEVFICVK
LKNTLDNAFE LQFEVRDTGI GIPPNKLNKL FKAFSQVDSS TTRKYGGTGL GLAISEKLVA
LMGGEIGVKS QVGKGTTFFF NITVKPGNKA QRNYVHLNLA EIQNKRILVV DDNQTNRDIL
EEQLKQWEFI PVMAESGTEA LKLLEDKEQV HLIISDMNMP EMDGITLARK IRELDGGIPI
ILLTSMGNEQ SKKNKSLFNV ALTKPTKHQV LYKHIIEQLK LTHEVKHEVQ PVKTPFSEDF
ANHHPINILI AEDNAINQKL AKYILNKMGY KPDLVENGHE CLNALINKKY DMVLMDVQMP
EMDGLEATRF IRQNMEHQPA IIAMTANAMA EDREQCLQAG MNDYLSKPLK LQEIMAALEK
WEPKKAAL
//
