ID A0A1M6CSN6_9BACT Unreviewed; 902 AA.
AC A0A1M6CSN6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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 ORFNames=SAMN02745146_1251 {ECO:0000313|EMBL:SHI63804.1};
OS Hymenobacter daecheongensis DSM 21074.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1121955 {ECO:0000313|EMBL:SHI63804.1, ECO:0000313|Proteomes:UP000184418};
RN [1] {ECO:0000313|EMBL:SHI63804.1, ECO:0000313|Proteomes:UP000184418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21074 {ECO:0000313|EMBL:SHI63804.1,
RC ECO:0000313|Proteomes:UP000184418};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQYN01000002; SHI63804.1; -; Genomic_DNA.
DR RefSeq; WP_073106623.1; NZ_FQYN01000002.1.
DR AlphaFoldDB; A0A1M6CSN6; -.
DR STRING; 1121955.SAMN02745146_1251; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000184418; Unassembled WGS sequence.
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; 2.
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; 3.30.565.10; 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; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; 1.
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; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
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; 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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184418}.
FT DOMAIN 42..79
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 277..347
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 419..643
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 665..783
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 802..899
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 714
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 841
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 902 AA; 97864 MW; 92CAFEE0C9815B19 CRC64;
MSDLSLPSAS PALPPTLAAA HHEILALRTA LAAAGQAPPA ATQTYLNILL SSLPNGLLLL
DENDRVVLVN DAYCRLLGLP LPAAGLVGMA SAELLPLVAA QLTDPAAFRA AAAAANGQQN
PDPNYKVAMP LLDGRTLELD FISHTDAHGN QLRLVHYCDV TERNRTQEAL HALARFPEQN
PNPVLRYGRE RQRLYANAAA ERLASEVPAD ELQQIRARLH DLTTQALDSG ETSRIELHSQ
GRYFNTCLVP NNDEGYVSIY MVDVTDLKQI QQALLDREKR YRDLQHYTQA MICTHALDGT
VLSLNPALTN LLGYSEQELA GRNMASVMPA EDQPGFAEYL ERIGRVGEEQ GVQRVQPQDS
DRIHYLLYHS VLVREANQKP FVIVHSHDIS ERIEGERALR QAKRAAEDAA RARTNFLANM
SHEIRTPLNG VLGMAARLDK TALNPQQREL VGIIRSSGQH LLTVINDVLD MAKISSGKLE
LNIESFNLCD SMGQAVQPLA LQAMEKGLRF EGTPLRDSCP YPWVLGDAHR LNQILINLVS
NAIKFTPVGG SVTVVGELLA ETAEELTVEF RVTDTGIGIA PEKLEHIFEN FTQAYADTAR
NFGGTGLGLS ISKALIQQMG GTLSVTSVPG QGSTFAFCLS LPRATALAQE IPTAAYDTGA
LRGRQVLLVE DNEINRVVAR LLLEEWGVVL DEAEDGPAAL RKFEQAPYDL VLMDIQLPGM
NGMAVTAAIR QHPDPVRAAV PIVALTANAF LSDAEQYLAA GMNDCVAKPF DENQLFEKLV
RLLKPAAPLY DLAQLQALAR GKQSFVQTLV RSFLHNVPTT LAGLQAAAAA ADHAELARLV
HYIKPNLIAF GISRALPLVA ELELLTAGPP APRVPAAVAE LTALLQQVLL ALPAELAAPE
LL
//
