ID A0A323V0C3_9RHOO Unreviewed; 833 AA.
AC A0A323V0C3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DNK49_09505 {ECO:0000313|EMBL:PZA16876.1};
OS Parazoarcus communis SWub3 = DSM 12120.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Parazoarcus.
OX NCBI_TaxID=1121029 {ECO:0000313|EMBL:PZA16876.1, ECO:0000313|Proteomes:UP000248259};
RN [1] {ECO:0000313|EMBL:PZA16876.1, ECO:0000313|Proteomes:UP000248259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWub3 {ECO:0000313|EMBL:PZA16876.1,
RC ECO:0000313|Proteomes:UP000248259};
RA Zorraquino Salvo V., Toubiana D., Blumwald E.;
RT "Azoarcus communis strain SWub3 genome.";
RL Submitted (JUN-2018) 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}.
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:PZA16876.1}.
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DR EMBL; QKOE01000005; PZA16876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A323V0C3; -.
DR OrthoDB; 8552871at2; -.
DR Proteomes; UP000248259; Unassembled WGS sequence.
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; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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; 1.
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; 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 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; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
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 Kinase {ECO:0000313|EMBL:PZA16876.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000248259};
KW Transferase {ECO:0000313|EMBL:PZA16876.1}.
FT DOMAIN 108..161
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 179..394
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 416..537
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 571..696
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 735..828
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 470
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 620
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 774
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 833 AA; 90170 MW; 081569F2A3730468 CRC64;
MTPASSSDVP QPEVPSLAQV RAQRDEAQGE LATLRDRLEL IKLGVYAGFW DLDLQDDRLE
VDVQWRDWLG YPAGGAGPDD WLSLVSADDR RLLRDRLVDH LRGVAEIFQV EFSLEAADGG
RRWLSVRGQA RERLADGRWR RVVGVYSDIS RERARELELL QAKEQAEAAS RAKGDFLANM
SHEIRTPMNG ILGMTELLLD SALAPEQRDY LQTVKSSAES LLTIINDILD FSRIEAGRME
LESIDFSMGA VVAETLRSLA LRAHQKGIEP YFTIAPDVPA VMRGDPARLR QVLVNLVGNA
IKFTERGEIE VAVRVLERRS GHVRVELSVR DTGIGIPADK QKAIFGAFSQ ADTSTTRKYG
GTGLGLTICQ HLVDLMGGRI ALDSQPGVGS CFRFDGRFPV VAEARPLKAP ALSGQRVLVA
AVNPAFAAAV CVMLARVGVA ASGVSGGQEA LLAFADAQRR NDPFAFVLMD ASMAAPGGFD
LAMRFQEAAP WLDRIVMMLD SHSQRNDIAR CNQLGLRSRL SKPFSAADLI DALQVALSGE
SADEHAMVAF EPERSLTEML REQQAPVRAL AILLAEDNPV NQTVATRMLE KVGHRVTVAN
NGEEAVEAFD AGNFDLILMD VQMPVMGGLE ATQAIRAREA RRSWAMQGGW HPIPIVAMTA
HAMAGDRERC LEAGMDDYVS KPIRPADLLA AIRRVSAPAD ADEDAEDSSL LDAQAAGVDG
GIANLDEARA LFDGDEAVVQ QLLAVFFRDL GSTLADLRGA GARNDLARLH EIAHSVKGSV
GLFGAQRATE AARVLDAAAK AGEPAAAGGL LEALIRELNM LASELRKQQR PAS
//
