ID A0A2M9BSI4_9BACT Unreviewed; 1375 AA.
AC A0A2M9BSI4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CLV45_2340 {ECO:0000313|EMBL:PJJ60905.1};
OS Hymenobacter chitinivorans DSM 11115.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1121954 {ECO:0000313|EMBL:PJJ60905.1, ECO:0000313|Proteomes:UP000228535};
RN [1] {ECO:0000313|EMBL:PJJ60905.1, ECO:0000313|Proteomes:UP000228535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11115 {ECO:0000313|EMBL:PJJ60905.1,
RC ECO:0000313|Proteomes:UP000228535};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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:PJJ60905.1}.
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DR EMBL; PGFA01000001; PJJ60905.1; -; Genomic_DNA.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000228535; Unassembled WGS sequence.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013767; PAS_fold.
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; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..64
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 165..236
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 240..292
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 293..363
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 660..712
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 713..784
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 784..833
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 851..1072
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1101..1219
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1278..1368
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 821..851
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1152
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1317
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1375 AA; 154441 MW; 5A9C30941EE4A850 CRC64;
MSTTPVSPAD AAALGTPPAP AADFYRVLFE EAYDAILLYD EQGGLVDCNQ TALRLLGTTR
PELLTTGLMA FAAPHAAAGA EAWQSAAELR AAVREVAHTG SRGARRWTGQ RPDATTVEAL
ATLHRVSSPE GGVRVQLTLR EAVETPAPAL SAADLITRQQ ALDLSQAQLR DLLSRTNLSY
VAVDRQAAVV DVNDHFLHYT EYSRSEVIGR SFHETFCPAA DQERMRQNFL TCIATEQLQE
FYERVIVTKS GQTRMVYWHA EFSRDLQGQV TGIFVVGRDY TDRHVAARAL TDNRHRLQDF
LDNAHDLIQN LSIDNRFLFV NKAWKEKLGF SDEDLSQMTL GDVVHPYYKA KLLYQLRNLY
KGEKVNKLET VFLTKTGKPI HLIGSISCSW QDDEPVSTRA ILHDITDRIK AERLQKVYYS
IANLAISSKD LQSLYGAIHR ELSKIIETNN FYIALCDDAR TQLQFSYFVD QNIQGEQGLV
SRPFSSGVSE YIIRTGRPMF MLKAELQELI ANGTITAYGL MPEVMLCSPL SIGERIIGVI
AVQDYHKADA YAAADIEILH FISNQVALAI ERKRNEVQIN KQNARLNAIF ESGSHLMWSV
DMHSRLTSFN RNYSAYFLRR NGVYPSLNVN LWQADLGMME EDAREAFIEN YRRAFQGQPQ
RFEVRLRDSR GQDTWREIYL NPIYLDDGTF EEISGMAHDI TDKKRSQLEL AAQEEKFRAI
FESFQDVYYR TDGKGVLTLL SPSVYDMLGY KPEEVIGTPI MDYYVRPEQR DELLNSIQNY
GEARNIEIDM RHKDGHSVSV LVNARQVNDG PAGTEGIGRD ITEFKQMQDD LRRAKEEAET
ALEAKTQFLA NMSHELRTPM NGIIGMIDLL HQTVASEEQE EYVDTLRKSS DALLAILNDI
LDLSKIQAGK LQLNESGIDL YYTLDKIHSL FANRANQKKL KFTYHITPHT PRFIITDETR
VLQILSNLTS NAIKFTSAGT VSIIVSSVST DGVEHTLRFA VQDSGIGISP SNAKLLFTNF
TQLDTTPTKA FGGTGLGLAI SKQLAELLGG EIGMISNTDD GSTFWFTMRC RVAYNEEEIV
QERVASRDRS HEIMRLETAP RVLLVDDNPI NQKVAVRLLD KLGCQIDVAN DGFEAISKAT
APTGEYELIF MDIQMPEMDG ITAMHEIRQR LGRSCPPIVA MTAYSMKEDA ERFVQQGMDD
YISKPVKSQD LYTVLLRWTG AAERMAALHL SAAPETPPTP DVTEPVAPYT PVGEALAEPA
QTTFIDPEVV KQLRELGGAE FAAQLYSDFE QEAGQLLSEA QQLVDQHQYA QILPHLHQLK
GTGFTLGINE LAECVKSLEH DLKKGHLDHV EQDFRTIMRH FTAFVHSYPA VTQGP
//
