ID A0A1Y0FYU2_9GAMM Unreviewed; 802 AA.
AC A0A1Y0FYU2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CBR65_14520 {ECO:0000313|EMBL:ARU28559.1};
OS Cellvibrio sp. PSBB006.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1987723 {ECO:0000313|EMBL:ARU28559.1, ECO:0000313|Proteomes:UP000196143};
RN [1] {ECO:0000313|EMBL:ARU28559.1, ECO:0000313|Proteomes:UP000196143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB006 {ECO:0000313|EMBL:ARU28559.1,
RC ECO:0000313|Proteomes:UP000196143};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; CP021382; ARU28559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0FYU2; -.
DR KEGG; cell:CBR65_14520; -.
DR Proteomes; UP000196143; Chromosome.
DR GO; GO:0016020; C: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; -; 2.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR033414; Sensor_dom.
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; PF17149; CHASE5; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ARU28559.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000196143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 188..246
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 285..507
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 529..647
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 671..792
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 220..266
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 583
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 722
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 802 AA; 90035 MW; 9502774192DA151B CRC64;
MLPTISRYAR ENPIATRLLG LIILSSSLIT LITILLQLYS SFHDDISSLE KRLDQVRIST
LASITKSLWG FDQEQLNIQI NSVLDVQDVV QVSVIWHDWN NTEQTLVAST QRYSQEDIDN
KPNQFLVKSY PLTYEDASTP QQQLGTLIIT ASLSSIYDKL WERALFIAGV QGAKTLLVSL
FILWLVHTLL TRHMDTIAQY ARQLNLDNLT TPLRLKRMKV DQHEDELDNV VNAINHMRET
LLEDIEQRHA IELALLSEKA EKLETRRLKN AAEDASRAKS QFLATMSHEI RTPMNGVIGM
LEMLRDTPLN DAQKHYVDVI HRSGETLLEI INDILDYSKI EAGKMQLEVA IFDLEDLIED
CIQLFGATAN KRRIELLGGV DPGTPLLLKG DPTRLRQVII NLLGNAFKFT SEGFISLDVK
LAPESTPEQP LLYFAVQDSG IGIDPTAYSM LFDSFNQADT STTRKYGGTG LGLAICKSLA
ELMGGHIGVD SIKGQGSTFW FTARFLPADI KSLAPHHDPA IDNLLHNRKL LLVDGSTKQR
QFLTKHGDSW GVILQEARSS ENALSILQEA AWRHEAFDFV IIDYHPGETS FAMVALMRQD
PVLKDTPIVL LSNVDVPQYH DQQLKIRNVL RKPVCARTIK LELAAILGVA IAPVSPQKQA
AQNYQLFSHL RVLVAEDNAV NRMVIKGLLG KLHIEPELVE NGVAAFNAVR ETATPYDLIL
MDCEMPEMDG FEATRSIREY ERSHNMPATP IVALTAHALQ EHREAVFASG MNHYLSKPIT
LDSLYTTFEK TGLMKTPEKN LR
//
