ID A0A2S8SP23_9BACT Unreviewed; 1352 AA.
AC A0A2S8SP23;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B1R32_1294 {ECO:0000313|EMBL:PQV62543.1};
OS Abditibacterium utsteinense.
OC Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC Abditibacteriaceae; Abditibacterium.
OX NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV62543.1, ECO:0000313|Proteomes:UP000237684};
RN [1] {ECO:0000313|EMBL:PQV62543.1, ECO:0000313|Proteomes:UP000237684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV62543.1,
RC ECO:0000313|Proteomes:UP000237684};
RX PubMed=29475572;
RA Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL Syst. Appl. Microbiol. 0:0-0(2018).
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:PQV62543.1}.
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DR EMBL; NIGF01000029; PQV62543.1; -; Genomic_DNA.
DR InParanoid; A0A2S8SP23; -.
DR Proteomes; UP000237684; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000237684};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 208..278
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 738..790
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 982..1199
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1231..1345
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1280
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1352 AA; 147774 MW; D0E8F80353BA43DD CRC64;
MKSAVTSGPF LMSKSSFVRR LLRFAWAVTL PLAAWSFAAC GRRIFARSGE AQRAISLEVP
SDEVGRYRAF LAQSTQAIWC FEFVPPLNIN QSEDEIIDQG YERGFLSECN DIFAHGCGFE
SAAPMIGMRL SDWLPREDPT NLARFRAFIR SSFRLNGAES VETTRDGEKH EFLNDLIGIV
EDGQLKRVWG TQHEVTAQKA AISELKASEA RFRALFDTAP VAISISREGV LMYVNRASVE
LLGCQNPDQM IGHAVSEFVA PTDRETMQER IAARASGSSM PLVYDALALR GDGKTLPLRV
EVTPLELPDG AATLGFAFDL SAERAVEAQR AEALAKERRT ALYAARLQQI TADLAASLTG
EAVAELIVSR GIAALDASAG ALSMPTQSER GPELEIIVGR GYPSHLTRNF KRLPVAENSP
LPAVRVLVEG RPVWIENAAQ AQRDFPVFSQ TLRDFEDQSV CLLPLEFEDQ ILGVLCLNFA
PPRPFDAEIR AFLLTLAGQC AQALERVRLA DEAQNAARLQ RESLALLNTL LETAPVGFAF
FDLQGRYVLV NEALAAMNCL PVEEHLGQKP RDILLSTGAR IAEAIDLVME SGKPSGEIEI
VSSGNNCGQE ICHSIAAFYP VRAGENEILG VGSVVIDISA RMSAERDRVQ LLGELEMERA
RFEAILHQMP SAVIIAEAPS GRLVLDNPQA EAVLGQHYAT AQSIAGYARY RGFHFDGREF
QAHEWPLARA LQKGEIVRGE EIMLRRDDQS TAVVRLNAAP IRDRDGHITA AVAIFDDVTQ
RAREGAAQRF LAEAGSALIS TLDERASYQQ LANLCVPNVT DWCIVAVPGN DGLLSQVAIA
CVNEDKKAVI EKFQSELAAD PQLPWDVGGA LRGRRAMLYP QHTIDWLLEM NTGAAYRRFI
EQIGAKSAIV TPLAARGRVL GTMIWISAES GRDYDDDDLQ LADEIARRAG LSAANARLYF
EAQTARHEAE NANRAKDEFL AVVSHELRTP LTPILGWLEL LRAPNAGEEI RTQAYSVIER
NARAQAQLIN DILDVSRITT GKLRFEFKPI ALHELIESVA ISLRPGATEK DIDFQLQIED
VGLARADANR IQQVVWNLLQ NAFKFTPKNG SVRVALQKSG GRAILEVQDS GQGIETAFLP
HVFDRFRQAD SSSTRRAGGL GLGLAIVAHI VEGHGGEVNA RSEGPGQGST FRVELPLLME
ELEPDSSLAP APFPLPEGEI KWENSLLQNI KILVVDDEPD TRQMLQMLLK TCGANVTLAV
SASDALQFLG ASTPDILVSD IGMALTDGYE LRREITRLGH ALPSIALSAY TAPSDVQKAL
DAGFDAHLAK PVDAEKLIFL IAQLARATKN QA
//
