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Database: UniProt
Entry: N9V4X3_9GAMM
LinkDB: N9V4X3_9GAMM
Original site: N9V4X3_9GAMM 
ID   N9V4X3_9GAMM            Unreviewed;       570 AA.
AC   N9V4X3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN   ORFNames=G114_18656 {ECO:0000313|EMBL:ENY70382.1};
OS   Aeromonas diversa CDC 2478-85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY70382.1, ECO:0000313|Proteomes:UP000023775};
RN   [1] {ECO:0000313|EMBL:ENY70382.1, ECO:0000313|Proteomes:UP000023775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2478-85 {ECO:0000313|EMBL:ENY70382.1,
RC   ECO:0000313|Proteomes:UP000023775};
RX   PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA   Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA   Fuste M.C.;
RT   "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL   Genome Announc. 1:S69-S82(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:ENY70382.1}.
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DR   EMBL; APVG01000083; ENY70382.1; -; Genomic_DNA.
DR   RefSeq; WP_005362807.1; NZ_CDCE01000037.1.
DR   AlphaFoldDB; N9V4X3; -.
DR   PATRIC; fig|1268237.3.peg.3653; -.
DR   eggNOG; COG3850; Bacteria.
DR   OrthoDB; 9811306at2; -.
DR   Proteomes; UP000023775; 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   Coiled coil {ECO:0000256|SAM:Coils};
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        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          176..228
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          370..566
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          220..247
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   570 AA;  64763 MW;  31C3F25C50189FBD CRC64;
     MKTWFEVRSV SSAIGRSMLL ILFMASLIAV VAMVTLFYSV PDAKAINLSG SLRMQAYRMA
     YEISKDQPVY SRLAQFEQTL HAGELQETQR WITPASLRRT YSRVLDEWQM MRLHIENDTP
     ERYSANTERF VSAIDDFVNE MQYHVEFKVR MLALAEGLGL LAIIVIAWFT VRFTRRQVVA
     PLNQLVACAR QIEQRNFHLY LPPRWPNELG ELSGAFATMA SELDKLYRDL EGKVEEKTAK
     LQQANDTLSF LYSTAQKLHE APLSSHTLAK LLDRAAAHQR IAHIRLTRFE RNAMPVYITG
     RTGWPGDIDG VEHFLLQMDE QEYGRLDLIS DFPIDQRLMK NFAMLLAQVV HKDQSLLQHQ
     RLLLMEERAV IARELHDSLA QALSYLKIQA TLLKRSFAKG QTQKAEQAMQ QIDEGLGNAY
     TQLRELLGTF RLTIGDLDLG EAIAVMLEQL KPQTQARIEL DYRLSSNDLE AGQHIHILQL
     IREAVLNAIK HANAQVIDVR CETLSDGTIQ VQVTDDGVGI GSSRSAVNHY GLSIMNERAS
     KLHGQLSISD RTPQGTCVHL IFPVLQTREP
//
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