ID A0A1B8TUW5_9FLAO Unreviewed; 1402 AA.
AC A0A1B8TUW5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LPB301_11080 {ECO:0000313|EMBL:OBY63358.1};
OS Polaribacter reichenbachii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=996801 {ECO:0000313|EMBL:OBY63358.1, ECO:0000313|Proteomes:UP000092612};
RN [1] {ECO:0000313|Proteomes:UP000092612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 23969 {ECO:0000313|Proteomes:UP000092612};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-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:OBY63358.1}.
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DR EMBL; LSFL01000035; OBY63358.1; -; Genomic_DNA.
DR RefSeq; WP_068361614.1; NZ_VRMM01000054.1.
DR STRING; 996801.BW723_04630; -.
DR KEGG; prn:BW723_04630; -.
DR OrthoDB; 1419493at2; -.
DR Proteomes; UP000092612; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 2.10.70.100; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 7.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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; IPR048533; VUPS.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 4.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF20973; VUPS; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 7.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000092612};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..330
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 468..520
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 521..568
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 725..777
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 866..918
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1001..1053
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1054..1119
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1306..1402
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1170..1197
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1402 AA; 161221 MW; 02F19DE3051E4D9B CRC64;
MNYTQIGILF FQASLIAFII LLLFRLRKRL GIGILFACLG LLQFLQVILS SAVYISITKN
LIVSPGSAVL FTATLFALLI IYIKEDTTET KKIIYALLVT NVLISVYLQV FGWSLGDTEN
NIANVNITFF DTNAWALFIG TILLFIDSLL IITIFEFISK KIRFLFLQIS ITMLIVLSFD
SISFTLLIFW NSESLNQILI SGIVSKAVFA LFYSVLFYVY LRYFELKSSP IKGVKIKDVF
QPLTYKQKYE SVAVGIKKAE EMYRLLADNS NDIICLQETD YSIKYISPSL NRILGYDSSY
FTENTFFDIV HSDDLNDFKK AKDQNLVQST IKSLPITSRF LHKEGHYIWL EFLSTPVYKD
DEINYFVTSI REVSQRVIDK QKIEESLKLL EEKENSLNEA SELAKIGYWE YINDSEEYTW
SEYIHHIYGS NPKEPTPSKV DILSKLDAKS QEKLKKVNLA LNTNGESYDI ELKLVNLKNK
IIWIRNVAQP IYNLDNKIIG KRGVLQDITE KKHTELKLIE NEEKFYNIFK SSPNLIILTR
LRDYKITDAN ETVLKATGYS IEEFLGNNFS PNDIWKSPDQ RKKYFDKLKE KGKINNFESE
FTTKSGEVRV WKTSSQIIKI SNEKYALSII EDITKIKQAQ YELQEKNEFI TAMTENLPAG
IIACNSEGKL VLFNKIAKDW HGIDVMNTPQ ENWASYYGLY ETDGKSMLKT EEIPLIRAFK
GEKIYNREIV IKSKNQEPRT VVCNGTSFSD SKGKTLGALV VMSDVTKQKL IENNLKQSEA
ETKKALKEIE RNEFLLNESG RLAKVGGWEL KLPSQEIRWS DEVFAIHGLP VGKVPPFEEC
VAFYIDGSDK LLAKAIQESI AQKKKFDLVL RFRNKKNQLL WVHSIGYPRI NKEGEITSLI
GVFQDITEQK TRQIKLDEQN EKLNKLNKVL NEAQALAHLG SWEYIAATGK VVWSEELLNI
FEMPAGSAAP NYDQHKKLYT AESFLKMEEG VANCLQYEKP YKLELDIYTA KGNLRHIISR
GKPIKDKNYN VIGCYGTAQD VTEQKKIRDN IARAEKMYRL LTDNSNDLIC LHKLDSTFKY
ISPSIKSILG YNEPELIETL GFNIIHKDDV NYFRESIEKR VLKLTPNDTF FCRAMHKKGY
SIWIECSISV IYLDNKIDFI LTSSRDVTEK IFAQQKIERY QESLQKLTTE ITLIEEKQKK
EIASNIHDHL SQSLVISNMK IKELRKLPEL QTIDEELGFI YEHISDALVN SRNITSELSP
PILYQLGIIE ALYWLLESIE TKHKIKGQIN ENIDKIILDD VQSILLYRSV QELLNNIIKY
AQATLITIDL NKTELGVDII IRDNGIGFNT EKLNNHYTKD EKGSGFGLFT VQERIKNIKG
EINISSIINK GTTVKIFIPI SN
//
