ID A0A2S5THU5_9GAMM Unreviewed; 1626 AA.
AC A0A2S5THU5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C3942_07065 {ECO:0000313|EMBL:PPE74517.1};
OS Solimonas fluminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Solimonas.
OX NCBI_TaxID=2086571 {ECO:0000313|EMBL:PPE74517.1, ECO:0000313|Proteomes:UP000238220};
RN [1] {ECO:0000313|EMBL:PPE74517.1, ECO:0000313|Proteomes:UP000238220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-BB {ECO:0000313|EMBL:PPE74517.1,
RC ECO:0000313|Proteomes:UP000238220};
RA Lee Y., Jeon C.O.;
RT "Genome sequencing of Solimonas sp. HR-BB.";
RL Submitted (FEB-2018) 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:PPE74517.1}.
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DR EMBL; PSNW01000003; PPE74517.1; -; Genomic_DNA.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000238220; 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; cd00130; PAS; 4.
DR CDD; cd00156; REC; 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; 3.30.450.350; CHASE domain; 1.
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; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
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 NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000238220};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..245
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 345..399
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 471..541
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 544..597
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 623..661
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 705..757
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 830..881
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 906..1127
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1148..1272
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1295..1413
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1446..1541
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 869..899
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1202
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1346
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1485
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1626 AA; 178627 MW; 3D3587FD3D066C4F CRC64;
MTKPGVIRPR TTAVALVAAG GAVVILASVL MVNASSRTRL QDAFDRAEKQ FVRQLDDRMR
KYEYGVRGAR GAAVVANSDG GLTLARFRDY ISTRDASREF PGARGFGFIR RVTRDSENAF
LEQARAEGRT DFSIRTLGPN SSDRYVIQYI EPEEINRRAV GLDIASDPVR LAAARRAMLS
GQATLTGPIP LVQAQSKEAN GFLLLLPVYR PGAPLRTEAE RFEATIGWSY APLIIDEILA
DLVAQDFGLA VSLSDVTPGA EASSFYSTSS ATIDAEFIQN TREFDVYGRR WQAVLTSKPS
LKQQTSVVPK PLAVLISLTL YLLLVALGIL VYRFRLRQRR ALADQLALTK GVIDAAPQAI
LVVDQTGVIL EANRQALTLF GYSLDALTGK SVDLLLPENS RDAHVAHRRR YDRLARPMAP
NRQLAARHFD GHGFPVEVSL SPLTLGRQEL VVASVTDVTE RLATLAHLQA SESRWRELAN
SMPQLVWTCQ GDGPCDFLSE QWVRYTGVPE AEQLGSGWLE QVHPDDRPQL MERWQAAVES
RGIFSVEFRI RRHDGIYRWF DTRAVPLLDP VSGAVVRWFG SNTDIEHRKQ AEEALRTLNA
TLEQQVVART QELREVLALQ GAILSNAGFA IIATEVDGTI KVFNPAAERL LGYAAAEVIS
KATPAIIHDP GEVAVRAESL SLELGYPVDV GFETFIAKAR LGAVDANEWT YVRKDGGRVP
VWLSVSALRR DDGELFGFLG MVVDITERRE LERTLRERER FLNEVTDSIP GMIGYWDSEL
HCRFANASYL SWFGRAKEQM IGIHIRDLLG EELFHRNEPL IRGALKGEAQ KFERRLKRAD
GSHGHTWAHY IPDMDGATVK GFYVLVTDIT ELKKAQEMLE ATNRILEQRN REVEAATQAK
SLFLANMSHE IRTPMNAVIG MLQLLQRTPM TRLQADYTDK AEAAARAMLA LINDILDFSK
IEAGKMQVER ELFKLDELLR QTGAVLSEML GAKDVEILFD IDPNVSSSLV GDKLRLQQVL
LNLAGNAIKF TERGEVVVGV HERERRGSVS VLDFFITDTG IGIAPEQMGK IFRGFEQAEA
STSRRYGGTG LGLAISRRLV ALMGGDLRVE STMGKGSRFW FSLEIELADT CPANLTSSNG
GVSLRDLRVL LVDDNPMARM VLRGYAESLG WRVEMASNGK EALALLETGS ISGIEHDVLL
IDWQMPDMSG WEICERIRSR PQPSKAALII MATAHGRGAL GEKLEQAPSL VDAFLVKPIT
ASMILDAVAD ARARHGTLWA QRAMVVSERR LDGARVLVVE DNTTNQQIAH DLLVSEGATV
TIANDGEAGV AAVRNGTPPF DVVLMDIQMP GMDGYEATRR IREYSARGRL PIIAMTANAM
PQDREACLAA GMNDHVGKPF HIDELVRVLR LHLRGDGVPG SLPARFQLSP KAEFNFPAAI
ARLGGKADLF ARQAKAFGVN HGSVAPELRA SLLAGDKLGA GRILHALKGV AGTLGAEGLA
DSAAMLELQI KEAGDQAVFN PDLMGLEGAL ARAVTELQRE ADRLSPDSKA VVPTRVSDDM
LRSNLIELMG LLAQNNTRAL ALLDLVIPAI EKLDSHAARE LRTFADKLDF AGALEACRKI
DLGGDE
//
