ID A0A0P7ZMX0_9CYAN Unreviewed; 1129 AA.
AC A0A0P7ZMX0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=chpA {ECO:0000313|EMBL:KPQ36384.1};
GN ORFNames=HLUCCA11_05855 {ECO:0000313|EMBL:KPQ36384.1};
OS Phormidesmis priestleyi Ana.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Phormidesmis.
OX NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ36384.1, ECO:0000313|Proteomes:UP000050465};
RN [1] {ECO:0000313|EMBL:KPQ36384.1, ECO:0000313|Proteomes:UP000050465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ana {ECO:0000313|EMBL:KPQ36384.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPQ36384.1}.
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DR EMBL; LJZR01000006; KPQ36384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ZMX0; -.
DR STRING; 1666911.HLUCCA11_05855; -.
DR PATRIC; fig|1666911.3.peg.5091; -.
DR Proteomes; UP000050465; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 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; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
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 PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KPQ36384.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:KPQ36384.1}.
FT DOMAIN 6..111
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 570..807
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 991..1116
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 383..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 383..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1041
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1129 AA; 123910 MW; 893C1E3F96FAD45A CRC64;
MGTGGMEDKE QEIRLQFLDE AGEYLDTLEA ALLGVAQRGV DSHEINSALR AAHSIKGGAA
LMGYALTSEL AHRLEDSLKV LKINRQMGVT ADVEGQMLNG VDMIRQVVEC DRTHTPIEDR
WVNDSVLPVF DGLTETLGEP AAEDAASMMD TDEGQNIMPL IFQTEVESLL ERLELLIDEQ
PSSLKSELIV MAQELGGLGE MLDLPSFVQL CASVEHYANS IATHTQLKEV SHQALQIWRR
AQALVLTDNV EAMPTELTNV SFGLIAIEFD EPQDEVDTSA ESVFAGFDID IDIEDEDAVD
LPLDDNLLAL GTEDEAVSGT EAVSNTVSDA FAERIDNPAP SQSSGFSDSF NSSVDQFSVD
QFSVDQSAVD QSAVDQFSVD QSAVGQSAGN QPIDQSVDQS VDQSVTGKST SSSSSSQSAT
EFRFSEGPQA QTEAADLGDH TVRVSVRKLN ELNDYFGELT IERNRLEAEV KRMRVLVKDL
SHKLRSLDEI NDDVRDLYER PERQLLLASG LNNPSSPSSP SDSSSPHLPT ANLPVASEIN
AATPQQPPTE SAPSPFRQEF DTLEFDRYND AHLPFRQIVE SVVKLQEVAD DIELSVDKTE
QTTRVIHRTA RHLQRNLNQL RMRPLSDVTN RFPRALRELE LAHGKSVSLA LEGESTLIDR
NILEALSDPL MHIVRNAFDH GIETPQARER QGKPRSGTIS IKAFNRSNRT VITVSDDGSG
IALEKIRDRA LSMGLDADLL DAASEAELLS LIFEPGFSTS EKVTALSGRG VGMDVVRNNL
TQIRGDISVD TAPGQGTTFT LSVPYTLSVT RVMLAEGSRM PVAVLTDFIE EVTIVKPEDL
FETEGREMFH FKGDAIHLIR LSNWLAFNCP RQFDSLEEVP NMDHPSVLLF RAGDQRLGLE
IDRSWGEREV AVRRVEGPIA LPAGFSNCTI LGDGKVVPLI NLPDFARWVL SCEASNIGSA
EALYSNPITQ GAIDPISLQT LPNAEMRRPA RFLVIDDSVN VRRLLVLTLE KAGYEVEQAR
DGQDAIDKLK NGIEVDGVVC DIEMPRMDGY SFLSKLRSFS ADDSPELAKL ADIPVTMLTS
RSGEKHRRLA MNLGATAYFS KPYQERVLLK SLAEGLAAAA ERKQPLADQ
//
