ID A0A060NMC5_9BURK Unreviewed; 1104 AA.
AC A0A060NMC5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SMCB_1468 {ECO:0000313|EMBL:BAO83696.1};
OS Serpentinimonas maccroryi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Serpentinimonas.
OX NCBI_TaxID=1458426 {ECO:0000313|EMBL:BAO83696.1, ECO:0000313|Proteomes:UP000066014};
RN [1] {ECO:0000313|EMBL:BAO83696.1, ECO:0000313|Proteomes:UP000066014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1 {ECO:0000313|EMBL:BAO83696.1,
RC ECO:0000313|Proteomes:UP000066014};
RX PubMed=24845058; DOI=10.1038/ncomms4900;
RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA Nealson K.H.;
RT "Physiological and genomic features of highly alkaliphilic hydrogen-
RT utilizing Betaproteobacteria from a continental serpentinizing site.";
RL Nat. Commun. 5:3900-3900(2014).
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};
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DR EMBL; AP014569; BAO83696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060NMC5; -.
DR STRING; 1458426.SMCB_1468; -.
DR KEGG; cbab:SMCB_1468; -.
DR HOGENOM; CLU_282654_0_0_4; -.
DR OrthoDB; 9176737at2; -.
DR Proteomes; UP000066014; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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; SSF55781; GAF domain-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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAO83696.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..299
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 303..356
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 583..804
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 845..964
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1012..1104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 968..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..59
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 351..378
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 894
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1051
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1104 AA; 120513 MW; 0F61E1D963F90231 CRC64;
MHIMKPSTPF ESKITLIFAG VVLVLLVLAY TALQLTRHAQ TLEKQVEHAQ EVLDTLNAIN
VHTLHIDVKR QNFIITGDQT LLPHLDVHRV HRGQALQRLR ELTQGNAAQQ EVWHQIRELL
DQRRAMSERI IELRLSAGEL AARRYSDDTP MLQTRVRLAE LLDTMEAHEQ RLLRTHQTKH
DRAQAINAYA YALLALLIAA LLLTTFWFIR RQLRANEAGR RALAASEQTL ATTLNSIGDA
VVATDTQGRV SLMNPVAERL SGWGFAAAQG QPLATVLHLI DEHSRAAVDL PVAQVLSSGS
SVGLSNHRLL LGRDGHEWPI TTTAAPIRGA EQQTSGVVLV LRDVSLERAA ARALRSQNEL
LEQRVRERTA QLQQKQRRQQ AENHVLDAIS SNQPLSAVLE TIAHEVEALM PDALCSILLF
DPEGVHLHHG AAPSLPAEFV RAIDGLQIGA QVGSCGTALH RNQQVIVSDI GTDPLWADFA
ALALPLGLRA CWSTPVRSGS TQVLGAFAVY YRSPRTPTAS ELEYLDDWSR LTGLAIERQR
DADAIEALNH SLERRVTERT AELELARLEA QRLSQVKDIF LATMSHEIRT PLNALFGMLE
LLGLRALDHE AQRMLGVALQ SGQALLHIID DILDFSRIEA GKLEIHPEPT SISELIELSA
DSFRKLSSSK GVRLLHWVDP QLSPLLLTDR LRLHQILNNL LSNAVKFTHA GQVTLKAERV
QLQGATERVR LSVTDTGIGI APAVQATLFQ PFSQGDAQTT RRYGGSGLGL AICRRLADLM
HGELELQSTP GVGTTLSLTL DLPILSAGEL QASPAAAWQP RRGSAPAACA FTPADRARER
AAGRLVLLVD DHPSNRDLLS AQLQTLGYAS DQANDGHEAL RLWECERYGL LITDCHMPDM
DGYQLMREIR RREAATGRVR LSILAWTANA LYDSSADCAA AGADDILVKP SNLLLLQQKL
EQLLPQDAPQ ADGAAAPADS TAADGPTAPP AQAPTQPPAL RRGALRELSG GDLALERTLL
LRFRAAHQAD AEALWRAAAA RDAAALAHLA HRIRGAALMI GADPLGNASL ALEQAAKEQD
WNAIEAALAA WKEAAAQLEP ELPT
//
