ID F6CRX4_MARPP Unreviewed; 1057 AA.
AC F6CRX4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mar181_3054 {ECO:0000313|EMBL:AEF56081.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF56081.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF56081.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP002771; AEF56081.1; -; Genomic_DNA.
DR RefSeq; WP_013797551.1; NC_015559.1.
DR AlphaFoldDB; F6CRX4; -.
DR STRING; 491952.Mar181_3054; -.
DR KEGG; mpc:Mar181_3054; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG3447; Bacteria.
DR eggNOG; COG3614; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_62_6; -.
DR Proteomes; UP000009230; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR007895; MASE1.
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:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:AEF56081.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AEF56081.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..412
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 562..783
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 934..1053
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 983
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1057 AA; 116063 MW; 854246AC5AE82AC4 CRC64;
MMTKIAKVIL LTALGYSVLG AVGLAVAVSP GYSTIIWPAS GLALVAVMFF PKYAPFGVFL
GSVLINVFIT WSNNQTFALA LPVCIAMGAT LQSCVGGYLV RRFVDVPRLF HRSRQAMRFV
VLGGVLSTLI GASIEASSLL FFGAIEYSQY WLNWSVLWAG DMIGVIFIVP WLAVFLPSLF
GGYFDRPMRL MNGLVVVLLI VAVLSWGGSY AEWNRQVKEF QSNAELLDVS ISNRVKNAVD
MLYSFVAFID GSEEINAEEF AFFSDRVMQR DDSIIGVSLN FSVAGNNISA FEKRIQRFYQ
DREFKVKERS LTGDLVAVTP RDRHIVMTFL SPLELNADAL GYDVYSQADR HFALDQAIQN
KQVYPTSPLR LVKDTKGVLL FLPFFDQQTD AFLGVASSII TLSTLTDTIV QKGRLPNTDL
YLVDEFGYGG EPVLVAKNMA ANLSVSDLLA TYEKGDFQHA VKADIRVGAK TWQLYQVSHS
YFFKQPWIVQ LVLAFSLFVA GLFGWFLLIV SSHAADVENK VRLRTKDLQL ANDSLKLSEL
KQSRAKDEAE QANRAKSEFL ANMSHEIRTP LNGVIGSLTL LLNSKLNPNQ THLATLSKHS
SESLLDVIND ILDLSKIEAG ALSIEAEPFL LSALVEEVTN IASLKAEEKG IILNVPATLV
PNLTLSGDRV RLKQVIMNLV GNAVKFTQVG EVNLTLTIDR QADDHHVLSF TVQDTGIGIS
EEAQSSLFQR FKQADGSTTR RFGGTGLGLA ISKEIVAAMG GEIRLESQKG VGSSFYVQIP
IQVSAIEAPQ TVSYDASVTL IYQNDTGRSY VVSVLDSLGC QVTSFGGLSE ALASDKGFER
LLLLDSDVLK KASSHDVDKL ERVCQEKQIQ QVLLQSRSAF EFSDSMMITS VMKPVFSKPL
LDVLESLKSP VLGEVMATKS NNAALENSPV FNAKVLLAED NLTNQIVARG LLNLYGVEVV
IAENGERAVT LAQQMTFDLV LMDCQMPVMD GYEATRHIRQ FDGTETPANV PIIALSANAM
KGDQDECFSA GMNDHIAKPV SQDKLVEALT KWLKQTD
//
