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Database: UniProt
Entry: A0A1R1DDR4_9BACL
LinkDB: A0A1R1DDR4_9BACL
Original site: A0A1R1DDR4_9BACL 
ID   A0A1R1DDR4_9BACL        Unreviewed;       637 AA.
AC   A0A1R1DDR4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BK133_04130 {ECO:0000313|EMBL:OMF37733.1};
OS   Paenibacillus sp. FSL H8-0548.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1920422 {ECO:0000313|EMBL:OMF37733.1, ECO:0000313|Proteomes:UP000187405};
RN   [1] {ECO:0000313|EMBL:OMF37733.1, ECO:0000313|Proteomes:UP000187405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H8-0548 {ECO:0000313|EMBL:OMF37733.1,
RC   ECO:0000313|Proteomes:UP000187405};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
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};
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:OMF37733.1}.
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DR   EMBL; MRTK01000004; OMF37733.1; -; Genomic_DNA.
DR   RefSeq; WP_076335107.1; NZ_MRTK01000004.1.
DR   AlphaFoldDB; A0A1R1DDR4; -.
DR   STRING; 1920422.BK133_04130; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000187405; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
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; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
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.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OMF37733.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187405};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          340..392
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          375..622
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   637 AA;  72634 MW;  E4530934BE71886C CRC64;
     MGRKCRAYVQ SIVNWLGRRS MQARLVAACI IILLIPSIGI SNYLFSQIED SYITDSLKQG
     QYSIEMEKVN ILNQIEAMER AAQLTISEHE ILEYVSREED LPVEELLELY RGPFTDMINI
     QINNPNIIHL RLYADNVHLS EVWPIIFHER RIQNESWFAK LDQLAGKELW MFSDQDPDIL
     HRNVTEGTDQ MPKVSLVRVI ESGGRRVASI QVEMLLKHFS PKAFASIKDE GSQMMIADGS
     GTVFLDENQP FASGNLELRQ AIVKEFAEMQ QQDITEKRFI VNQLPYLLVT TDLEQVDAHI
     LNVVSLQASS ERISKAAKQI IAVNVISIGL LSIIMYIMNS FILKNLRRLT EAMKKVRRGE
     MPTGLPLGGG GEIGELAHHF NKLIHTINEL IAQGVRKQAL TKEAELRTLH SQIDSHFLYN
     TLENIKMLAE MENQRTISDS LTSLGGMMRY NFKWSGEYVS LQDEVRHIQN YIAVMNIRFD
     EPIHLELHIP PRLLEIEVLK MSLQPIIENT VKHAGFGAEA SNSTIRIDVA ENEEANIVIT
     LRDNGRGISV SRLEQLNERI HLDRNNELSL TQENINVKQT FGIGLQNVHQ RIQLYYGEQY
     GLQVYSSEGQ FTEVVITLPK VLLMGGSSGY EENDNRR
//
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