ID A0A0C1ICP6_9BACT Unreviewed; 2007 AA.
AC A0A0C1ICP6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HY58_05790 {ECO:0000313|EMBL:KIC91730.1};
OS Flavihumibacter sp. ZG627.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1463156 {ECO:0000313|EMBL:KIC91730.1, ECO:0000313|Proteomes:UP000031400};
RN [1] {ECO:0000313|EMBL:KIC91730.1, ECO:0000313|Proteomes:UP000031400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZG627 {ECO:0000313|EMBL:KIC91730.1,
RC ECO:0000313|Proteomes:UP000031400};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter carbonis ZG627.";
RL Submitted (JUL-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:KIC91730.1}.
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DR EMBL; JPHF01000002; KIC91730.1; -; Genomic_DNA.
DR STRING; 1463156.HY58_05790; -.
DR Proteomes; UP000031400; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 10.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 7.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
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; 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; 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; PF00672; HAMP; 7.
DR Pfam; PF18947; HAMP_2; 4.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 11.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 4.
DR PROSITE; PS50885; HAMP; 11.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000031400};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 103..160
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 200..252
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 292..344
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 384..436
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 476..528
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 568..620
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 660..712
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 752..804
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 844..896
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 936..988
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1028..1080
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1320..1553
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1619..1732
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1741..1858
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1888..2005
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1054..1081
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1251..1310
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1668
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1791
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1938
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2007 AA; 220768 MW; 22C14EC2E9E5A892 CRC64;
MNPSDVQNDH DDSLSDAELL KVLTEVKNGN FSIRMPFDKL GISGKICDTL NEIISLNEIL
TQELETAKHT IGKQGKLNHR VELPRSARGS WNSSVESINT LISDLVHPTI EIAHVISSVA
NGNLSQEMPQ KIGDHLLQGE FARIAKEVND MVKQLNLFSM EVTRVAREVG SEGKLGGQAR
VKGVAGVWKD LTDSVNQMAG NLTAQVRNIA EVTTAVAKGD LSKKITVDVE GEILELKNTI
NTMVDQLNSF SSEVTRVARE VGTDGKLGGQ AEVKGVAGTW KDLTDSVNQM ASNLTDQVRN
IAQVTTAVAK GDLSRKITVD VKGEILELKN TINTMVDQLN SFSSEVTRVA VEVGSEGKLG
GQATVKGVDG VWKDLTESVN QMGSNLTAQV RNIAEVTTAV ANGDLSKKIT VDVQGEILEL
KNTFNTMVDQ LNSFASEVTR VALEVGTEGK LGGQAKVQGV GGTWKDLTDS VNQMASNLTA
QVRNIAEVTT AVANGDLSKK ITVDVAGEIL ELKKTINTMV DQLNSFASEV TRVALEVGTE
GKLGGQAKVK GVGGTWKDLT ESVNQMGSNL TAQVRNIAEV TTAVAKGDLS RKITVDVKGE
ILELKNTINT MVDQLNSFGS EVTRVAREVG SEGQLGGQAD VPGVEGLWKD LTDSVNKMAS
NLTSQVRNIA EVTTAVANGD LSRKIEVDVK GEILELKNTI NTMVEQLRSF ASEVTRVARE
VGTDGKLGGQ ANVPGVGGTW KDLTDSVNQM AGNLTDQVRN IADVAIAVAK GDMSRKITVD
VRGEILQLKE TLNTMVDQLR AFASEVTRVA REVGTDGKLG GQAFVPGVAG IWKDLTDSVN
HMTGNLTDQV RNIAEVTKAV ASGDLTKKVT IDVKGEIFEL KNTINTMVDQ LTSFAYEVTR
VAREVGTEGK LGGQAEVKGV AGTWKDLTDS VNMMAYNLTN QVRGIAKVVT AVATGNLKQK
LSIVSRGEVA QLTDTINEMI DTLALFADQV TTVAREVGVE GRLGGQASVP GASGIWKNLT
ENVNQLAENL TTQVRAISDV ASAVTQGDLT QMITVEAKGE VEELKDTINQ MIANLKQTTL
RNQEQDWLKS NLAKLTQMLQ GQKDLKTVTR HILSELAQVV NAQKGMFYIL EQDENLQNKK
LKLYAAYAFD KEIALKKEFS LGEGLVGQCA LEKERILLTN IPRNYSKIVS GLGNSTPANL
IVLPVLFETE IKAVIELASF DHFSETHLDF LTQLTESIGI VLNTIEANSR TENLLQQSQS
LTDELRRANE ELQDKAHLLV KQKEEVEAKN KEVEEARLSL EEKAEQLELT SKYKSEFLAN
MSHELRTPLN SLLILAQQLY ENHEGNLNDK QVRYAKTIHS CGDDLIQLIN DILDLSKIES
GYISTDFINV KFNQITSFVE TTFKHVSESR NLRFSIEKQD GLPEGFETDS QRLNQILKNL
LSNAFKFTEK GEVKLRIYEA DRGWKHSNPE LDSARRVVAF EIRDTGIGIS KDKQNIIFEA
FQQAEGSTSR KYGGTGLGLS ISRGLADLLG GTIELESEAG RGSVFTLYLP MESATQPVRR
EKPTSKKKRE FKISEISEFI SKEVTNSEKL TENNELEGLN EIINDIGDDR NNIIPPDKVV
LVIEDDERFA RIMIEKAHEK NMKAVVATHF ADVFELANKF NPVAITLDVK LPDASGWRIL
DLFKTDINLR HIPVHLVSGE ENRVLAMQRG ARSFHLKPLK AEGLTMLFND MQEFSSRKEK
KLLIVEDNET ESAQLAKFLD NNDIISIDIA NTGNEALELL HKNAYDCVVV DYMLPDIAGL
DFVIEASAIN KLRMTPLLIY SARDFSIKEK GRLKHYASKI MLKNINSLDL LLEEIVTLLH
IDHQDLTPEK RTLIEELRSS KDILINKTVL VVDDDVRNLF ALTTSFERYH INTITAESGQ
EAMDILNEND KIDIVLMDIM MPEMDGYETT QKIRREHKNT TLPIIAVTAK AMKGDREKCI
EAGASDYITK PVKMDQLLSL MRVWLYK
//
