ID   A0A074MCM6_ERYLO        Unreviewed;       782 AA.
AC   A0A074MCM6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=EH31_00690 {ECO:0000313|EMBL:KEO91214.1};
OS   Erythrobacter longus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO91214.1, ECO:0000313|Proteomes:UP000027647};
RN   [1] {ECO:0000313|EMBL:KEO91214.1, ECO:0000313|Proteomes:UP000027647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO91214.1,
RC   ECO:0000313|Proteomes:UP000027647};
RA   Zheng Q.;
RT   "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL   Submitted (APR-2014) 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   -!- 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:KEO91214.1}.
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DR   EMBL; JMIW01000001; KEO91214.1; -; Genomic_DNA.
DR   RefSeq; WP_034957497.1; NZ_JMIW01000001.1.
DR   AlphaFoldDB; A0A074MCM6; -.
DR   STRING; 1044.EH31_00690; -.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 9797304at2; -.
DR   Proteomes; UP000027647; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 2.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KEO91214.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027647};
KW   Transferase {ECO:0000313|EMBL:KEO91214.1}.
FT   DOMAIN          567..782
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   782 AA;  84726 MW;  4FE7FE5E8C2EA5BB CRC64;
     MELTPPALIV IALLLAAWTI AAAVLVLRAG AKTSRAKALQ TSLRRMQHLI DVAPAIPLLV
     RTDGRIEAPE RLARWLGLSQ IPAYLSELVG EDGEGLSRPQ VDELWEKVRT TQKSASPFSM
     TVTPPGSQRS LALEGSLADA QVSPGGAAIV WVFDFTASES ELARLSEEAS NAKSDFASLS
     GLIASAPTPM WIRDTDMNIR LANEAYIEAV GADSLEAVIE GQIELLEARD GQSPAQIAME
     AYQSKKQIDR IDGVTIDGER RSMRVTDLPL GEDGVAGYAI DVEEQQQLAR DFRAFREAQR
     SMLDQLSVGV AQFAPDETLS FANRPFRRLF GLFSNDALEG KLLFSRLLSD ARERGQTPEV
     RDFPEWREEH RSWFDASETQ EENWPLPGGM HLRIVAQPMP DGGLVMIAED RTEQLALSAT
     RDTLLRTRTA TLDSLIEALA IFAPDGSVQL WNRSFAGTWG LSGEFLDTHP SAQDLLGAIG
     SNLQDPYETE AIGAVVRAAT LDRQEKQGQV RLSDGRTLRF AGAPLPDGNG LLTVLDVTDS
     QKAEQALRDR AKALEEADAV KARFLANMSY EFRTPLTTIG GYAELLASGA AGEMNEAASE
     YVDAILTSAA RLTEQVENVL DLSQTEAGLM PITKEDVDLL PFLTALVRER ETAIVKAGIG
     LDLKGRRGRM VEADPRQLGR AVGNLIDNAI AGTPEGGKIT IQLPKPARED DWRGRIIIQD
     DGCGMSREQL ERAMGASSQP EEPGEGAGLG IRLAHQLVAA HGGMLELDSQ EGVGTIAMIT
     LP
//