ID R9PL70_AGAAL Unreviewed; 1272 AA.
AC R9PL70;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AALB_2197 {ECO:0000313|EMBL:GAD02117.1};
OS Agarivorans albus MKT 106.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Agarivorans.
OX NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD02117.1, ECO:0000313|Proteomes:UP000014461};
RN [1] {ECO:0000313|EMBL:GAD02117.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT Marine Bacterium.";
RL Genome Announc. 1:e00367-13(2013).
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:GAD02117.1}.
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DR EMBL; BARX01000013; GAD02117.1; -; Genomic_DNA.
DR RefSeq; WP_016401885.1; NZ_BARX01000013.1.
DR AlphaFoldDB; R9PL70; -.
DR STRING; 1331007.AALB_2197; -.
DR Proteomes; UP000014461; Unassembled WGS sequence.
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; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000014461};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 72..127
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 128..182
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 205..255
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 256..334
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 337..389
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 476..529
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 547..768
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 787..905
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 933..1049
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1092..1194
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 840
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 982
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1131
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1272 AA; 141680 MW; 819193F23BBC1EEB CRC64;
MKKPLWDLYE FAPIAYASVD KEGRFLQHNL SFSELIEVER DGFEALSFHD FAENQEQRQK
SKELLAAAFV GHSFNDEVLS IFTSSGQKKT VSINIVPSLD EEGHIHVVKV SLIDMTERYQ
ARLALADNEE RIRTIVDTIA DGIILIEQSG IVRSFSPAAE QIFGYSEAEV IGKNVKMLMP
SDIGDQHDRI LADYKPKKES SVIGNEREVF GLRKNGEQFP MELAVKEVFL KGQRHFTGVV
RDITARRKAQ QKLADSERQF RTLTNNLQCV VYRIRLKEGE YPEWLYISEQ IEEQTGYPIS
DFVGLNPVRR YKELVHPDDA EESLARSREL NQKGGAISQE FRIIDASGKV KHMLQKAFVS
MDEEGRPAYS DGAIFDISEI KQVEAQLRES EERLDSAASG AGLGMWDYYP QEDRIEVNAI
YESMLGYAKG ELRDGDGLWA RLKGDTATWM KLIHPSDVIT NNEKLEQHLA GENDVLRNEI
RLRCKNGQYR WILTIGRVSE LDEHGKPLRI NGIHVDIEET KKLEAALNEA RALADSANQA
KSDFLANMSH EIRTPMNAII GMSYLALETE LDNKQRNYID KVHRSAEALL GIINDILDFS
KIEAGKLDIE KIDFRLEDIL DNLANLVGLR AEQKSLELLF DIDPSIPTAL IGDPLRLTQI
LVNLCNNAVK FTEQGVVVVK IEAKQQDNKQ VQLYFSVSDT GIGMTPEQQA KLFKPFSQAD
SSTTRKHGGT GLGLAICLKL TELMGGKIAL SSELGQGSCF YFELPMQIQE NAQTLRDTNS
AQLSSLKALV VDDNANARDI NQQVLESFGL EVESASSGSE AIALIKEHAE TSAFDMVFMD
WKMPDMDGVQ TVQHIQDQGF DLDVIMVTAF GRDELTKEAE AVNIDAVLTK PVTPSHLFDT
IVQVRKIEVL EQTRREAQQQ GANLDIAQLQ GANILVAEDN DVNQELITEL LGSNGLNCTV
CDDGSQAVEY LKENKVDGVL MDCQMPVMDG YTATKVIRYQ LGLKELPVIA LTANALAGDR
EKAIEAGMND HIPKPINVNS LFSTMAKWIT PASPTTVNQS GQSAKVANDQ DLKLPEIDGL
DTEAGLANAA DNKALYLKLI GKFANEENTP MDDLNTAYTE ERIDELQRIA HTIKGVTATL
GGQAVSDLAA VVEQQAEENT VQPSSIEALG KQLIPLQQSL QEFVSQVETT EIAEEGALQS
VSEEELLSYL QQLAQLLDDF DGESNDYLDS HDCILQTFPA QAKKLQMLIE EYDYEAAGEI
VQEMQQQVTK KA
//
