ID A0A1M5JMD0_9BACT Unreviewed; 2141 AA.
AC A0A1M5JMD0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04488109_0144 {ECO:0000313|EMBL:SHG41420.1};
OS Chryseolinea serpens.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Chryseolinea.
OX NCBI_TaxID=947013 {ECO:0000313|EMBL:SHG41420.1, ECO:0000313|Proteomes:UP000184212};
RN [1] {ECO:0000313|EMBL:SHG41420.1, ECO:0000313|Proteomes:UP000184212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24574 {ECO:0000313|EMBL:SHG41420.1,
RC ECO:0000313|Proteomes:UP000184212};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQWQ01000001; SHG41420.1; -; Genomic_DNA.
DR STRING; 947013.SAMN04488109_0144; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000184212; 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; 11.
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; 12.
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; 5.
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, ECO:0000313|EMBL:SHG41420.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184212};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 233..285
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 325..377
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 417..469
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 509..561
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 601..653
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 693..745
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 785..837
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 877..929
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 969..1021
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1061..1113
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1153..1205
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1452..1685
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1755..1868
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1877..1992
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 2022..2139
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1179..1206
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1383..1442
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1804
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1926
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 2072
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2141 AA; 232822 MW; 29AD50BEC06DBF9B CRC64;
MKTKAALKEK RTPAKKSASN VRVKKNGSNG HDTDSLHADG HAISSDQIGS KELLRVLTEV
KNGNFSVRMP IDEVGLNGKI YDTLNEIISL NEKMMQEFTR AGNTIGKQGK LTQRIEIPST
KGAWSEGVNS LNVLISDLVH PTIEIAHVIS SVAKGNLSQE MPEEIGDHRL EGEFLRIAKE
VNYMVKQLNL FSMEVTRVAR EVGSEGKLGG QAKVKGVGGV WKDLTDSVNH MAGNLTNQVR
NIAEVTTAIA RGNLSKKITV DVKGEMLELK NTINTMVDQL NSFSSEVTRV ALEVGTEGRL
GGQATVKGVG GVWKDLTDSV NQMAGNLTAQ VRNIAGVTTA VATGDLSKKI TVDAKGELLE
LKNTINTMVD QLNSFSSEVT RVAREVGSEG QLGGQADVPG VGGTWKDLTD SVNQMAGNLT
NQVRNIAGVT TAVANGDLSK KITVDVRGEM LELKNTINTM VDQLNSFGSE VTRVALEVGT
EGKLGGQATV KGVGGIWKDL TDSVNQMASN LTGQVRNIAG VTTAVANGDL SKKITVDVRG
EMLELKNTIN TMVDQLNSFG SEVTRVALEV GTEGKLGGQA TVKGVGGVWK DLTDSVNQMA
GNLTAQVRNV AGVTTAVAKG DLSKKITVDA KGELLELKNT INTMVDQLNS FSSEVTRVAR
EVGSDGQLGG QANVPGVGGT WKDLTDSVNQ MASNLTNQVR NIAEVTTAVA KGDLSKKIAV
DVRGEMLELK NTINTMVDQL NSFGSEVTRV AREVGSEGQL GGQADVPGVG GTWKDLTDSV
NKMADNLTNQ VRNIAEVTTA VAKGDLSKKI TVDVKGEMLE LKDTINTMVD QLNSFASEVT
RVAREVGSEG KLGGQATVKG VGGVWKGLTD SVNQMAGNLT AQIRNIANVA IAVANGDLSK
KITVDVRGEI LQLKDTLNTM VDQLRGFASE VTRVAREVGT DGKLGGQAFV PGVAGTWKDL
TDSVNQMAGN LTDQVRNIAG VTTAVANGDL SKKITVDVRG EMLELKNTIN TMVEQLNSFA
FEVTRVAREV GTEGKLGGQA EVRGVAGTWK DLTDSVNQMA SNLTGQVRGI AKVVTSVAKG
NLKQKLSINA LGELAQLTDT INEMIDTLAV FAEQVTTVAR EVGVEGRLGG QASVPGASGT
WKDLTENVNQ LAANLTTQVR SISEVASAVT KGDLTRTIRV DAKGELEALK DTINQMITNL
RETTLRNQDQ DWLKSNLAKF TQMLQGQKDL KTVTRRILSE LAQVVSTHYG AFYILQQDED
MAQVKLKLFA AYAYKEERTI PREFAIGEGL VGQCALEKEK ILLTNVPQGY VKINSGLGRA
KPANLIILPI VFENNVKAVI ELASLDVFNE THLDFLDQLT ESLGIVLNTI ETNTRTEELL
AQSQSLAGEL KTQQEELRRT NDELQDKAFL LVKQKDEVEA KNKEVEEARK SLEEKAEQLT
LTSKYKSEFL ANMSHELRTP LNSLLILAQQ LYENAEGNLN DKQIRYAKTI HSCGDDLIQL
INDILDLSKI ESGFISANIS SVRIGEIASF VETTFKPISE ARNLKFKIET DYTLPATMDT
DIQRLNQILK NLLSNAFKFT EKGEVALKIF EAQRTWKPGV ATLDNASTVV AFSISDTGIG
IPQEKQLIIF EAFQQAEGST SRKYGGTGLG LSISRGLAEL LGGTIELDSE AGRGSTFTLY
LPLNSLASAA PRQVSESIKV IQELQLDNDG NQINNLLGNL RITNEGVEAR NMDIVNEMIN
DSGDDRSHIQ ANDKVVLVVE DDLRFGKIVI EKAHEKGLKA VVATNYLEVF DFINRFSPIA
ITLDVKLPDT SGWKVIDLLR NDLTYRHIPI HVISGEENRV LALKRGARSF LLKPLNNDLL
NNLFNDIVTY DRKEKKSILI VEDNELDSSQ IAKMHRDDKV DVTIAGTAKE ALELVQAEEF
DCIILDYTLP DMPGSELLHE VSRAKADLTP VIVYSAKDFS KTEMSNVNLN SSSHIVKGVN
SIEYLLEETI SHLHINHKSL APEKRRIIEN IRNKEDILTG KNILVVDDDV RNLFALTTVF
ERFNINVITA ESGREAINIL TENPKIEMVL MDIMMPEMDG YETTQKIRRE HKNNTLPIIA
VTAKAMKGDR QKCIEAGASD YITKPVKIDQ LLSLMRLWFC K
//