ID A4U2M2_9PROT Unreviewed; 1036 AA.
AC A4U2M2;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MGR_1840 {ECO:0000313|EMBL:CAM77129.1};
OS Magnetospirillum gryphiswaldense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM77129.1};
RN [1] {ECO:0000313|EMBL:CAM77129.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSR-1 {ECO:0000313|EMBL:CAM77129.1};
RX PubMed=17449609; DOI=10.1128/JB.00119-07;
RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA Reinhardt R., Schueler D.;
RT "Comparative genome analysis of four magnetotactic bacteria reveals a
RT complex set of group-specific genes implicated in magnetosome
RT biomineralization and function.";
RL J. Bacteriol. 189:4899-4910(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU459003; CAM77129.1; -; Genomic_DNA.
DR AlphaFoldDB; A4U2M2; -.
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; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 16..132
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 145..215
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 470..540
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 547..597
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 629..763
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 772..1026
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
FT MOD_RES 67
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1036 AA; 113167 MW; 0F32604063C6F692 CRC64;
MRHLHRTMNG SAQLKRLLVI EDNPGDQRLI EIKLAEAMPG WKADCRATLA DGIAMAISTD
YTCILADLGL PDAAGLTSVL RLTEAAPDKA LVVLTGLDDE RVAQDAIRAG AQDYVVKSLA
GLDMLPRVIR HAIERQQSRT ALELSHQTAQ ALLDASHDMA MLLDEDGHVI TLNAQAAEAF
GRRSEELEGM DVFTLMPPDL ADRRRAFFAK ALESGRTIQS EDNDGPRWFT HRFLAVGAEG
AARRCAIFSR DISGERAAAA NLEAAKEEAE LANRSKTEFM GRMSRDIRTP LNDVIGFSEM
IATEMLGPLA PSGYREYGET ILASGSQILK MLDRITDVSM LESALLKDQS SYRDLVELSP
DLICVCVDGA IERINAAGLG LLRAPAASAC EGKPFVDFIH PDYRGLFDMG IEALYEEDHP
VPVKVVTFAG RVRDVEINAV PLRRDGHTAA LLVGRDTTEV TAAMRAVAAR EHRIRAIMDT
VLDGIVTIDE DGLIVSANLS VERIFGYPLS ELIGANVSIL MPEPDAGRHD SYIKNYLQGQ
GGGLIGSGRE VMARRKDGSL FPVHLSVSEL RLDKRRLFTG TIRDLTENKQ LAQRVAYLAN
HDSLTDLPNR TLLCDRLGQA LAAARGTGQH VAVMTIDLAG FTMINDSLGH DVGNGVLRET
ARRLAQWVSL HNGTAARLAG DEFAVILPGL RDLAGVSAGT EQVLEMLNRP MTVGGSDLAL
PVDIGVSVFP RDGDEPLDLL RNAEMALHQV KKREDQRLGF FDTAMSYAVS ERLTLERSLK
EALKAGQFEL FYQPQVRLSD YALIGAEALI RWRHPELGTI APDKFIPVAE ETGLIVPLGR
WVLEQACRQL NLWQHQGLTQ VRMGVNISGR QFREVDLAET VAEVIRGSGI DARLLDLELT
ESMLMADGES TLRVLRRLAD LGVTLSIDDF GTGYSSLAYL KRFPVHTVKI DRAFVRDLDH
DEDGRTIAKA IVSLAHSLNL KTIAEGVETE AQASLLLHHG CDEIQGYLIG RPMPVADFAV
FAAGYDGSSW AKGGKA
//
