ID A0A076HS89_9BACT Unreviewed; 1159 AA.
AC A0A076HS89;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=N008_05705 {ECO:0000313|EMBL:AII51477.1};
OS Hymenobacter sp. APR13.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1356852 {ECO:0000313|EMBL:AII51477.1, ECO:0000313|Proteomes:UP000028590};
RN [1] {ECO:0000313|EMBL:AII51477.1, ECO:0000313|Proteomes:UP000028590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APR13 {ECO:0000313|EMBL:AII51477.1,
RC ECO:0000313|Proteomes:UP000028590};
RA Li P., Jiang J., Kwok A.H.Y., Lou X., Xu D., Leung F.C.C.;
RT "Complete genome sequence assembly of Hymenobacter sp. APR13.";
RL Submitted (JUL-2013) 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; CP006587; AII51477.1; -; Genomic_DNA.
DR RefSeq; WP_052381234.1; NZ_CP006587.1.
DR AlphaFoldDB; A0A076HS89; -.
DR STRING; 1356852.N008_05705; -.
DR KEGG; hym:N008_05705; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_15_10; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000028590; Chromosome.
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; 3.
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; 4.
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; 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; 2.
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; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
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; 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
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:UP000028590}.
FT DOMAIN 333..386
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 516..587
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 589..641
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 659..882
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 904..1019
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1057..1154
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 570..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 953
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1096
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1159 AA; 129589 MW; B6C98A41E0A2F1E0 CRC64;
MNSIPPSFLS ETGRSAFALL ESLFDALVLL SPDGQVRWAS AGFGRLTGVA EVPAVAALLR
EGLAGAGVSP AAFQQQLAGA QPLHYTLELR QATGSHVPVR LKLAPHEAGL LGLLEVLPPA
SAPTGEQQEQ EARLSYLAGQ APGVLFQWRE GQGPTAGLRY VSAQLEPLFG LNPQQAHMLP
HLLHPTDAYR WRRAASRTRR LGEPFAFEGR LLVPGQPVRW LRASAQLSGT DATGALYSGL
LTDITPLKQA EEAVFNQEQR WRQAMERFGD GAWEFDYATG EEYFSQAYHA MLGYTPDSPE
PLPASWEQHV HPADRALSLE AADAYLRGEK PLYSVERRLR CRDGSYKWVL TRGLVTQRDA
QGQPRTMTGV HTDISAVKET TLALEASMLR FSTTIANFQE GILLEDEHQQ VVLANDALCQ
IFALNTTPDQ LVGYNTRLLG QRMQHQFRHP EAFAQRYATI VRERQLLTAE LFELANGHVI
QGDFVPIYVA ERYIGHLWKF QDITERKRND DALRQREEKY RGIIENMNMG LVEMDLNRRV
LFVNQAFSDI TGYDRASFTE HHTIDRLMSP EDVAQARQRD QRRRRGESET YEISITDSAG
ELKWLLVSAA PLYDEDRQVY GSIAIVLDIT HQKALELNLR AAKEQAEDSA RAKELFLANM
SHEIRTPMNA ILGMGQLLAK TPLDTVQHTY LQAIETSGEN LLVILNDILD LSKIGASQLH
IERIGFSLAE LLLQVEKSLH FKAEEKGLVF RVVLDERLPA VLLGDPYRIT QVLLNLAGNS
IKFTEKGSVT ITCTQACTDD THVELQWSVA DTGIGIDAEY LVDIFKDFSQ EDPSVTRRFG
GTGLGLSISR QLVQLMGGEI SIDSQKHRGT NSQFRLRLPI GTTQDLPRKT LITASVREKL
RGQRVLLVED NHFNRQIAKG FLHNAGLQVQ EAENGAEAVE IARHHSFDAV LMDVQMPVMN
GLEATAYLRQ HLRLPTPIIA LTANAVKGER EKCLHAGMND YLSKPFQEDD LLKVLCLWTL
GEQLPEATAL PSAAAATTAG PGTLYNLDIV RQIGQNDVSF TILMLESFIE SCREAVEELR
TAIAEQDILQ IRMAAHKLKP SLDHLQVYRL LPLVVELDTW RTPFDAEHLP QLVEQVVAQL
QELTWQMQLE LQTLQPELE
//
