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Database: UniProt
Entry: A0A0P1EJQ9_9RHOB
LinkDB: A0A0P1EJQ9_9RHOB
Original site: A0A0P1EJQ9_9RHOB 
ID   A0A0P1EJQ9_9RHOB        Unreviewed;       582 AA.
AC   A0A0P1EJQ9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=arcB_2 {ECO:0000313|EMBL:CUH50767.1};
GN   ORFNames=SHM7688_00196 {ECO:0000313|EMBL:CUH50767.1};
OS   Shimia marina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH50767.1, ECO:0000313|Proteomes:UP000054823};
RN   [1] {ECO:0000313|EMBL:CUH50767.1, ECO:0000313|Proteomes:UP000054823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH50767.1,
RC   ECO:0000313|Proteomes:UP000054823};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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};
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DR   EMBL; CYPW01000002; CUH50767.1; -; Genomic_DNA.
DR   RefSeq; WP_058238161.1; NZ_FOMU01000014.1.
DR   AlphaFoldDB; A0A0P1EJQ9; -.
DR   STRING; 321267.SHM7688_00196; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000054823; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 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   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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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; 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   PROSITE; PS50109; HIS_KIN; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054823};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH50767.1}.
FT   DOMAIN          216..437
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          462..582
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         511
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   582 AA;  63942 MW;  8DF7021E41BF031E CRC64;
     MKSSFFSSWK DILEIQNAFL KQAQSDLPVE DLLKSLTDRL DALHDRHAVS VMLKGEGETL
     IFAAGSRLSS DYIDQINPLP YGPNVGSCGT AAFEKKQVIV DNMLTHPLWA DFRHLQPACG
     YMASWSQPML SKDNSLLGTF AVYFKEPRAP SEMETDIIES LGNTVGFILE RKKYEDTLKT
     TNASLAKKVA ARTAELELQK EKAEEANTLK TRFLAAMSHE LRTPLNGIIG AGNLLSNSKL
     NKEQCELNEM SVNSAQLLLT LVNDLLDLST IESGEFKLNL EPGNLRQNLE EVCALFHVSG
     KAKQVPINLS ISETVSARYA LDYMRIKQII FNLVGNALKF TSDGSVEIRV SEAPADTTPT
     SLRFEVEDNG IGISKDHHQT IFQLFRQADA STTRKYGGTG LGLAICKKLI EGMGGQIGVE
     SQLGEGARFW FEIPATTCNV SVKENASNTL EVAGITATAR RQVLLVEDSA VNRTIATKLL
     ETLNCEVDTA QNGKESLDLI EGKTYDLVFM DCMMPEMDGY AATKIIRERE QTSSAPTTLP
     IVALTANAMH GDEEKCLSAG MTDYLTKPFD AKSLEAMLSK HI
//
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