ID A3HUT2_9BACT Unreviewed; 603 AA.
AC A3HUT2;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Oxygen sensor histidine kinase NreB {ECO:0000256|ARBA:ARBA00017322};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Nitrogen regulation protein B {ECO:0000256|ARBA:ARBA00030800};
GN ORFNames=ALPR1_01645 {ECO:0000313|EMBL:EAZ81904.1};
OS Algoriphagus machipongonensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=388413 {ECO:0000313|EMBL:EAZ81904.1, ECO:0000313|Proteomes:UP000003919};
RN [1] {ECO:0000313|EMBL:EAZ81904.1, ECO:0000313|Proteomes:UP000003919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR1 {ECO:0000313|EMBL:EAZ81904.1,
RC ECO:0000313|Proteomes:UP000003919};
RX PubMed=21183675; DOI=10.1128/JB.01421-10;
RA Alegado R.A., Ferriera S., Nusbaum C., Young S.K., Zeng Q., Imamovic A.,
RA Fairclough S.R., King N.;
RT "Complete genome sequence of Algoriphagus sp. PR1, bacterial prey of a
RT colony-forming choanoflagellate.";
RL J. Bacteriol. 193:1485-1486(2011).
CC -!- FUNCTION: Member of the two-component regulatory system NreB/NreC
CC involved in the control of dissimilatory nitrate/nitrite reduction in
CC response to oxygen. NreB functions as a direct oxygen sensor histidine
CC kinase which is autophosphorylated, in the absence of oxygen, probably
CC at the conserved histidine residue, and transfers its phosphate group
CC probably to a conserved aspartate residue of NreC. NreB/NreC activates
CC the expression of the nitrate (narGHJI) and nitrite (nir) reductase
CC operons, as well as the putative nitrate transporter gene narT.
CC {ECO:0000256|ARBA:ARBA00024827}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {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:EAZ81904.1}.
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DR EMBL; AAXU02000001; EAZ81904.1; -; Genomic_DNA.
DR RefSeq; WP_008197945.1; NZ_CM001023.1.
DR AlphaFoldDB; A3HUT2; -.
DR STRING; 388413.ALPR1_01645; -.
DR eggNOG; COG4585; Bacteria.
DR HOGENOM; CLU_039270_0_0_10; -.
DR OrthoDB; 9760839at2; -.
DR Proteomes; UP000003919; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF13675; PilJ; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAZ81904.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Reference proteome {ECO:0000313|Proteomes:UP000003919};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..376
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 406..603
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 603 AA; 68380 MW; 46A383503F4CFC05 CRC64;
MAQHTKTLDQ YTFNRLRRLY IIALGAIAIS LLTSQFLIRT YLNDQEDDSK LINVAGRQRM
LSQKLTKEVL LLTLNKSDST KQPLIENIHA TQAEWEMAHQ ALKFGDEKLG LEAENSPEIS
EMFAGIQPTF DQVITTTQSL ILLSQKPSPD SVLVNQELKK LQGAASAFLK QMEKIVDQYD
NEAKAKVSKL RKLEIGITIF TLLVLLGEFL IIFWPSAKAM KNSIRELMEA EKKAVKMAKD
ADLLSQSKEK SVRELRALSQ AMDEILLFAR VTPEGYVTHM GDQFARLLQA KKLNLNAKFS
ELISINENEQ LMVDRIISEN KKSGWQGEIK ACNKEGTEIW LDFSMLPFNA GENKTELIIV
CLDITKRKEA MLEVERLTKE SFEEKMLQQK VLSRQIIENQ ENEQNRIAKD IHDGIGQMLT
GLKYLLESVE LENPESAAEK IEKLKLLTSN IIKGVRTATF NLTPPELKDY GIVPALTELT
QELEKLTDKN IVLFNKTDFN QRLDSLVEIN LYRITQEAIN NAIKYADSSH IIVTISHSEK
LLSIIVDDNG KGFDKSKLKA KPDKDGGMGL TFMQERINYI NGRLFINSSE NEGTRVTLNV
PLQ
//
