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Database: UniProt
Entry: A0A0Q9S918_9BACL
LinkDB: A0A0Q9S918_9BACL
Original site: A0A0Q9S918_9BACL 
ID   A0A0Q9S918_9BACL        Unreviewed;       603 AA.
AC   A0A0Q9S918;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=HAMP domain-containing protein {ECO:0000259|PROSITE:PS50885};
GN   ORFNames=ASG93_08730 {ECO:0000313|EMBL:KRF21452.1};
OS   Paenibacillus sp. Soil787.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF21452.1, ECO:0000313|Proteomes:UP000051948};
RN   [1] {ECO:0000313|EMBL:KRF21452.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF21452.1,
RC   ECO:0000313|Proteomes:UP000051948};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF21452.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF21452.1,
RC   ECO:0000313|Proteomes:UP000051948};
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   -!- 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:KRF21452.1}.
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DR   EMBL; LMSP01000023; KRF21452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9S918; -.
DR   STRING; 1736411.ASG93_08730; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000051948; 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; IPR003660; HAMP_dom.
DR   InterPro; IPR036890; HATPase_C_sf.
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; PF06580; His_kinase; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        300..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          322..379
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
SQ   SEQUENCE   603 AA;  68545 MW;  F2D5E492C22903AD CRC64;
     MRNKLILFLL LATLIPFITS IVVSYFFTKQ KVIEDTIASN AVLISQGKTN LLNYLNGVLQ
     ASSTIYTGTG PPVYGLGQIY DILERQQEID YMSDKVISSG LQVMSHSVKE IKQVYLYAGV
     SNRSYLMVNN NSKSSSGKYE NLPSFPENKD VYFETTHSSS NYGIHTVYSA PTPVLSMHRK
     LLYSPNNTTI GELIIDLQLD LISEISQSLY THDQEELYIL DEAGFIVFGP DISKWGQLLE
     GSWGNEAIHS KLDKGTYEWS KGPYAGINVY EKMKTDYVSW TIVKRLPYEQ LTRNARQLTL
     INSMILTLFM LIVIAGTIYI SIKFTAPIKQ LIRYITRIQS GQVQLGQLNV DIELARTDEM
     GILANRFHGL MQDLNQMVMR EYRLELANKS NQLMALQAQI NPHFLNNALQ SIGTLALQHD
     APKVYALISS LAKMMHYSMN TNESVVPLRK EIDHIKAYLE LQKQRFEHQF EIIYDIEEST
     KAISVPKMIL QPLVENYFKH GFKPGSATGL LRIQAMKDIV HEDEFLKLIV EDNGIGITEQ
     RLYEVRNRLN APSITDEACI GLSNVLTRVQ LYFTDDAFLD VEHVQPQGLR IMIHIPMKKG
     ALE
//
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