ID   K6DWF8_9BACI            Unreviewed;       908 AA.
AC   K6DWF8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=HAMP domain-containing protein {ECO:0000259|PROSITE:PS50885};
GN   ORFNames=BABA_21141 {ECO:0000313|EMBL:EKN65191.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65191.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN65191.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
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:EKN65191.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJLS01000137; EKN65191.1; -; Genomic_DNA.
DR   RefSeq; WP_007087220.1; NZ_AJLS01000137.1.
DR   AlphaFoldDB; K6DWF8; -.
DR   STRING; 1117379.BABA_21141; -.
DR   PATRIC; fig|1117379.3.peg.4384; -.
DR   eggNOG; COG2972; Bacteria.
DR   OrthoDB; 2482518at2; -.
DR   Proteomes; UP000006316; 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   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; 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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000006316};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        13..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        616..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          635..689
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   COILED          670..716
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   908 AA;  105257 MW;  A7A5A123C544DADE CRC64;
     MKKTMGNLPF HTFLLRFSLI TVFVFLLLLS SLYYMKIKNF IEEKKETSVQ LRMDQISTEL
     QTEFNNIYDT VNNLKTNEIV IRYLDELGDN NLSPSEKYKQ LSNLEEYLYT IRQNNKLIDN
     ILIVTPETQF SSDMKYIDYQ YNGMKLNNEA ERQYHFVSIG EANRKIEIPS ISGGQAVEAS
     GSKDLNNSMF FGVNILSADG VNKGVILIFI NPKNLDDYIF YADHIGLFDQ NGRLFFKGDK
     AVDNLPAKLK KLPSSKKGLQ GTYENTGIYH SSIPYYNFQL VYVEKLSFYK KQMALMWKML
     VATFLFSALI AYIFSRIVGR KVLQPLDRLI ESIKGYEESR NYSSLFQQKK NRVMKVSLRE
     RFFFYFVITV LLPLVIFMVM LYGQTSKIIS SDLQESYRAS HEKMARLMNN EINQRVLLLT
     RIAYNNNVLH SMMEEDAESI GHELLNKKQY LELRRQTVKI YNLEGKPIYT NGYSENKQMD
     PHFLMQLQAT GRNISYTLEK NHFNDVTIVI GMPAFSVADN AKSIGYITVD MEGNELAKFY
     ADWQKTGLNM LLADQHNRIL SHPDPLKIGT IVSDKESGTN YHIFKKEITG MDWKFISTYN
     DSAIQKQIEQ LFISDAYLLA LVLLLLLAFA YWISKRMLRP IGQLNSLFHT FDLQGSHHEV
     VEQLSGISEM DSLTQNFNKM VERMEELIHE TILADQERIQ LKYEKRELQL NALQSQINPH
     FLYNTLDNLI YLVESSETER ALEMIASLSK LFRFITNREQ VMITLRDELV YTKTYIKIMS
     YRFDNFECVW DGDEKILSYK TVKLILQPVI ENAIHHGARK TKNRVTIHIS CKLIEDQIHI
     IVKDNAIGIR EDDLAIIKNH LTSATLDKAG IYNVNGRIRL HFGNQYGLDI ESIWGEGTTV
     TIVIPAAM
//