ID S5S7G3_RHIET Unreviewed; 641 AA.
AC S5S7G3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=REMIM1_PF00212 {ECO:0000313|EMBL:AGS25880.1};
OS Rhizobium etli bv. mimosae str. Mim1.
OG Plasmid pRetMIM1f {ECO:0000313|EMBL:AGS25880.1,
OG ECO:0000313|Proteomes:UP000015261}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=1328306 {ECO:0000313|EMBL:AGS25880.1, ECO:0000313|Proteomes:UP000015261};
RN [1] {ECO:0000313|EMBL:AGS25880.1, ECO:0000313|Proteomes:UP000015261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mim1 {ECO:0000313|EMBL:AGS25880.1,
RC ECO:0000313|Proteomes:UP000015261};
RC PLASMID=Plasmid pRetMIM1f {ECO:0000313|Proteomes:UP000015261};
RA Rogel M.A., Bustos P., Santamaria R.I., Gonzalez V., Romero D.,
RA Cevallos M.A., Lozano L., Ormeno-Orrillo E., Martinez-Romero E.;
RT "Genomic basis of Rhizobium etli symbiovar mimosae and its prevalence among
RT Phaseolus vulgaris nodule bacteria.";
RL Submitted (MAY-2013) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP005956; AGS25880.1; -; Genomic_DNA.
DR RefSeq; WP_020919252.1; NC_021911.1.
DR AlphaFoldDB; S5S7G3; -.
DR KEGG; rel:REMIM1_PF00212; -.
DR PATRIC; fig|1328306.3.peg.6308; -.
DR HOGENOM; CLU_000445_114_51_5; -.
DR Proteomes; UP000015261; Plasmid pRetMIM1f.
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; cd16919; HATPase_CckA-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd18161; REC_hyHK_blue-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AGS25880.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:AGS25880.1};
KW Transferase {ECO:0000313|EMBL:AGS25880.1}.
FT DOMAIN 15..64
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 137..207
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 277..499
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 523..638
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 573
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 641 AA; 70176 MW; 184A52A95EB1C4DC CRC64;
MPHRLVSPRT ASPQELDAMV HVLDGADILV HRFDGTITHW SIGCENMYGW AREEAVGEKV
YDLLATKFHE PAENIRDQLR SRGFWQGEII HRHKSGHEIH VASRCVLVKL PDGEFAVIQT
NSDVSALRGA QEAVKAREAH LSSILDTVPD AMVVIDHKGT VLSFSKAAEK LFGMPSDQIC
GRNVSNLMPN PYRDAHDGYI DHYIETGEKR IIGYGRVVTG QRADGSQFPM ELHVGEATAN
GERIFTGFVR DLTSRFKIEE DLRQAQKMEA IGQLTGGLAH DFNNLLTVIS GNLEMIEDKL
PPGSLRDILR EAQAAAQDGA ILTGQLLAFG RRQPLNPRHA DLGQLVTGFA DLLRRTLGED
IKLSTIIDGS DLSVLVDSSQ LQNAILNIAL NARDAMPKGG SLTTTISRVH LDADYAKMYP
EVRSGNFVLV TMTDTGMGMT EEVRKRAIEP FFTTKEVGSG TGLGLSMVYG FVKQSGGHLQ
LYSEVGRGTT VRIYLPAVAG AKPREPAPDH GVGESQLPRG DETVLVVEDD ARVRRVAVAR
LASMGYTVLE AENGRRALDL LRENSDIALL FTDIVMPGGI TGDELAREVR VLRPDIAVLF
TSGYSEPGLA GKGIVPGAQW LRKPYTAREL ALKIRELLDT K
//
