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Database: UniProt
Entry: U1H219_9PAST
LinkDB: U1H219_9PAST
Original site: U1H219_9PAST 
ID   U1H219_9PAST            Unreviewed;       571 AA.
AC   U1H219;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN   ORFNames=N561_05915 {ECO:0000313|EMBL:ERF78481.1};
OS   Gallibacterium anatis 12656/12.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Gallibacterium.
OX   NCBI_TaxID=1195244 {ECO:0000313|EMBL:ERF78481.1, ECO:0000313|Proteomes:UP000016529};
RN   [1] {ECO:0000313|EMBL:ERF78481.1, ECO:0000313|Proteomes:UP000016529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12656/12 {ECO:0000313|EMBL:ERF78481.1};
RX   PubMed=24115542;
RA   Kudirkiene E., Christensen H., Bojesen A.M.;
RT   "Draft Genome Sequence of Gallibacterium anatis bv. haemolytica 12656-12
RT   Liver, an Isolate Obtained from the Liver of a Septicemic Chicken.";
RL   Genome Announc. 1:e00810-13(2013).
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         ECO:0000256|PIRNR:PIRNR003167};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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:ERF78481.1}.
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DR   EMBL; AVOX01000023; ERF78481.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1H219; -.
DR   PATRIC; fig|1195244.3.peg.1147; -.
DR   Proteomes; UP000016529; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd22899; NarQ_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 1.20.120.960; Histidine kinase NarX, sensor domain; 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; IPR029095; NarX-like_N.
DR   InterPro; IPR042295; NarX-like_N_sf.
DR   InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF13675; PilJ; 1.
DR   PIRSF; PIRSF003167; STHK_NarX/NarQ; 2.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 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|PIRNR:PIRNR003167};
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR003167};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR003167};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003167};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003167};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003167};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003167};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW   ECO:0000256|PIRNR:PIRNR003167}.
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          178..231
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          370..569
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   571 AA;  65151 MW;  53D48C3DBA164EAA CRC64;
     MEKNVAKYSV LTRVAKYLIG IILLASFCIS LVFTLLISSQ SDAEAINLAG SLRMQAYRLI
     YQMEHEQDTV AHNLQQYTQT LQEKTLNDLQ NSYFVPANVK AAYQNVVNNW QQMSSFVRQQ
     QINQYQAQVD QYVAKVDDFV AELQHFSERK IIMAILISIF SIITILVIGS YMLWYMKREV
     LNPIEKLVQA STQVQTGHFK HIPLDVDKPN ELGTLSETFT KMASELQKLY WFLEEKVSEK
     TKKLSQLNRT LSMLFHTSQK ITHIDLDYNQ LTEVISEIRA SEHLRYIELI VYGAEHLDLS
     SGKAEDNYPW QEQKISVNGK LLSCLRWQAG LPCPDLRLMQ SVAQMLGRAI YFIQTQRQQQ
     QLVLMEERSI IARELHDSLA QVLAFLQIQL TLLKHALKSS DPQAKEKSFK IIADFEQALN
     DGYVQLRELL STFRLTIQEA NLKLALEQVI ESLRNQSDAQ ITLECSLPSQ IFTAQQLVHA
     LQVVREALLN AIKHSQATLI EVIAHTNQDG ENEIIVADNG IGIPSLDEPE GHYGLNIMQE
     RTAQLNATLT IQRRPTGGTE VKILLANTFT E
//
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