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Database: UniProt
Entry: F2JVM9_MARM1
LinkDB: F2JVM9_MARM1
Original site: F2JVM9_MARM1 
ID   F2JVM9_MARM1            Unreviewed;       458 AA.
AC   F2JVM9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Marme_1300 {ECO:0000313|EMBL:ADZ90573.1};
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS   MMB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ90573.1, ECO:0000313|Proteomes:UP000001062};
RN   [1] {ECO:0000313|EMBL:ADZ90573.1, ECO:0000313|Proteomes:UP000001062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC   {ECO:0000313|Proteomes:UP000001062};
RX   PubMed=22675599; DOI=10.4056/sigs.2545743;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA   Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA   Sanchez-Amat A.;
RT   "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT   mediterranea type strain (MMB-1(T)).";
RL   Stand. Genomic Sci. 6:63-73(2012).
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; CP002583; ADZ90573.1; -; Genomic_DNA.
DR   RefSeq; WP_013660478.1; NZ_CP047696.1.
DR   AlphaFoldDB; F2JVM9; -.
DR   STRING; 717774.Marme_1300; -.
DR   KEGG; mme:Marme_1300; -.
DR   PATRIC; fig|717774.3.peg.1348; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_133_5_6; -.
DR   OrthoDB; 1931120at2; -.
DR   Proteomes; UP000001062; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF56; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADZ90573.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001062};
KW   Transferase {ECO:0000313|EMBL:ADZ90573.1}.
FT   DOMAIN          216..450
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          162..207
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   458 AA;  51107 MW;  8A88C3B6A6920306 CRC64;
     MKHQKYLSKL LRNSVIDSGN IHEASNVVLS AYVRASYLKD GSIWLLDDNG SMVCSFILDN
     HDSSPSPFSS MDETQVQALI DSLNNLPYLT LDRAQLTSAY WVSNIDLVNH TLILTPVFYK
     GQMVGLIQGR RQAHQPEFDN DDIQFAIALA DIFGRVILAT QNNKLQHALK NANLELEQKI
     LKRNTDLKKT LEDLQTAQNH LVESEKMAAL GQLVCGVAHE VNTPLGVAIT SLSILGDEVN
     KLKNAYDAGT LDESTFMAFV ESAKSAHDIA EVNMHRAATL VREFKQTSVD QSHRALIKLD
     LKTLIESIIS SLTPIYQPYR VEFAIDIPEN ITITTYSESI DQILTNLINN SCIHGFRESD
     RPHNLIYIKV FIQKDDFVID YQDNGVGIDD AIAKNVFTPF FTTNRSNGGS GLGLSVIYNL
     ISQKLKGDIR VVEQDASLGA HFQIRLPRTL TLDQESET
//
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