ID A0A0Q9N876_9BACL Unreviewed; 604 AA.
AC A0A0Q9N876;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASL11_05250 {ECO:0000313|EMBL:KRE74762.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE74762.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE74762.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE74762.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE74762.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE74762.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KRE74762.1}.
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DR EMBL; LMSD01000003; KRE74762.1; -; Genomic_DNA.
DR RefSeq; WP_056610539.1; NZ_LMSD01000003.1.
DR AlphaFoldDB; A0A0Q9N876; -.
DR STRING; 1736398.ASL11_05250; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000051252; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..377
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT COILED 365..399
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 604 AA; 69377 MW; 16746EC2C904F1F6 CRC64;
MNLNKKVFIG FLLFIIIPLF VLGSAVYTVS QQLIEKKYGD LTEVTLQAIS RNIYYMFKEA
NYFSDFWMVK DSIQGIYRTI DATKPNADPL SSYDLNTFDT LLRGSILTYS PVQSVVIYNN
SGKSFSAGRT SGSSIPWQTI QQSMAFQHIQ ELNGSPLWIG PSEFKEFGSG RGEFYQARMV
KDFWTMDNLG YMLLKFKFNE LDQIFKSFNT SEQNSKRYLL INKNGLIFYD NKQSLEGANV
LQLTQGKLDL GFNNYSFKAD FQNEKSLISL YHLNINGMGV QDWSVVSITS WKYVAGEIET
IMKLVAGITF ICLFFALVYN LVFVRRIIQL ILRMLSSMKK VERGDLTTRL EVSGKDETTA
LARGFNSLVV RIEDLLEEVK RQQDRKNKAE LMLLQAQIKP HFLFNTLESI NVLAIQNQGK
KVSQMVIRLG NLLRIGMENR EEITLKQELE HLRSYLEIQE FRFEDQFQYT IEAPPELLHE
DILKLTLQPL VENSLQHGFE PIDYMGVISV KVVDEGDRIG LYVTDNGVGI SNEKLAKFHY
KTELETPFHE ILESNEERRG LGVSNVADRV RIQYGEHYGM FICSQEGQGT TMKVIIPKRK
RDAG
//
