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Database: UniProt
Entry: A4U0R1_9PROT
LinkDB: A4U0R1_9PROT
Original site: A4U0R1_9PROT 
ID   A4U0R1_9PROT            Unreviewed;       697 AA.
AC   A4U0R1;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MGR_3195 {ECO:0000313|EMBL:CAM76468.1};
OS   Magnetospirillum gryphiswaldense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM76468.1};
RN   [1] {ECO:0000313|EMBL:CAM76468.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MSR-1 {ECO:0000313|EMBL:CAM76468.1};
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};
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DR   EMBL; CU459003; CAM76468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4U0R1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF46; C4-DICARBOXYLATE TRANSPORT SENSOR PROTEIN DCTB; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 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; 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; 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   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          195..259
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          265..315
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          328..551
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          571..686
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         620
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   697 AA;  76469 MW;  18E27EB5614939D3 CRC64;
     MIAHSVADQL RQIDRAVTTL TRSTEALLRA TDEKTLLEHI CRIAVEVAGF KLAWVGYAQN
     DDAQSVTPMA VAGWRTDYVD EIGASWGEGI RGHGPIGNAI RTGVTQITVD TEIDPRFAPW
     REAVRKHGFR SCIALPLAQV AERIGALVIY AGEPDAFDAD IVRLLEDLAR NLSYGIGTLR
     MRVEHDRAVR ELAESEERYR SLIELTPDAI LVHSMGEILF ANPAALQVFG NGLSSLVGES
     ILQLIPPEEH PILIERFTRP PPGRVRAEHQ MIRLDGSLFD AEVVATTITF HSRPARLLVI
     RDISDRREVQ EQLVQTAKLA TLGEMAAGLV HELSQPLNII RLTAEGALLF IERGKATQEW
     QAQQFHLIAD QSQRTAEIID DIRIFSRRDN SPMQVFDAMS ATRSAMAVLE GQLRPDEITL
     VTRLPDTPIP VRGRRVQLEQ VIMNLLSNAH HALKEKREHN GGGKAWAAEI AVTARQDGNR
     LTIRVADNGP GIPPAVRARI FEPFFTTKEA GRGTGLGLSV SFGIINAMGG RLELDSAGLG
     ACFVISLPID SDDEPQAVPQ SPPQTCPIDA HIMVVDDETT ATETLGRYLT EMGYRVTLCG
     SGSEALTRFR DDPADVVITD LRMPSGGGEQ LVEQLREYDP LQPIVIVTGH LGATERLAEN
     LQDDRCAVLK KPVALGKLGE IIATFLLPPG DEEFTQT
//
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