ID D0SDU1_ACIJO Unreviewed; 493 AA.
AC D0SDU1;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=DNA-binding transcriptional regulator NtrC {ECO:0000256|ARBA:ARBA00019059, ECO:0000256|RuleBase:RU365013};
DE AltName: Full=Nitrogen regulation protein NR(I) {ECO:0000256|RuleBase:RU365013};
GN Name=ntrC {ECO:0000256|RuleBase:RU365013,
GN ECO:0000313|EMBL:EEY95601.1};
GN ORFNames=HMPREF0016_02014 {ECO:0000313|EMBL:EEY95601.1};
OS Acinetobacter johnsonii SH046.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575586 {ECO:0000313|EMBL:EEY95601.1, ECO:0000313|Proteomes:UP000012047};
RN [1] {ECO:0000313|Proteomes:UP000012047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH046 {ECO:0000313|Proteomes:UP000012047};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
CC -!- FUNCTION: Member of the two-component regulatory system NtrB/NtrC,
CC which controls expression of the nitrogen-regulated (ntr) genes in
CC response to nitrogen limitation. Phosphorylated NtrC binds directly to
CC DNA and stimulates the formation of open promoter-sigma54-RNA
CC polymerase complexes. {ECO:0000256|RuleBase:RU365013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU365013}.
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DR EMBL; GG704967; EEY95601.1; -; Genomic_DNA.
DR RefSeq; WP_004696552.1; NZ_GG704967.1.
DR AlphaFoldDB; D0SDU1; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_1_6; -.
DR Proteomes; UP000012047; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19919; REC_NtrC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR010114; Transcript_reg_NtrC.
DR NCBIfam; TIGR01818; ntrC; 1.
DR PANTHER; PTHR32071:SF15; DNA-BINDING TRANSCRIPTIONAL REGULATOR NTRC; 1.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|RuleBase:RU365013};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365013};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365013};
KW DNA-binding {ECO:0000256|RuleBase:RU365013};
KW Nitrogen fixation {ECO:0000256|RuleBase:RU365013};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365013};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|RuleBase:RU365013};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU365013};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU365013};
KW Two-component regulatory system {ECO:0000256|RuleBase:RU365013}.
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 142..371
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 493 AA; 55658 MW; 9C00FCDC385060FE CRC64;
MSRNKIWVID DDRAMRWVLE KTFKEEGFDV TSFEEAQSAL DQLSLDAPDV ILTDIRMPGI
DGLTFLAKVK ANYPDLPVII MTAHSDLESA VSSYQTGAFE YLPKPFDIDE ALALVNRAIL
HITKMQQQES AKTVPPIQST EIIGESPAMQ EVFRAIGRLS QSHITVLING ESGTGKELVA
HALHRHSPRS SKPFIALNMA AIPKDLIETE LFGHEKGAFT GANTQRQGRF EQANGGTLFL
DEIGDMPFET QTRLLRVLAD GEFYRVGGHI PVKVDVRIVA ATHQDLEKLV HDGRFREDLY
HRLNVIRIHI PKLAHRSEDI PMLAQHFLAR AGKELGVSPK ILRPETQEYM QQLPWQGNVR
QLENTCRWLT VMITGREVYP EDLPSELKQI PITRSGEDAQ AAQNLDRIAV HHWDELLGQW
AVQKLKNGEM KILDIATPMF ERTLIIAALQ QTRGRKRHAA ELLGWGRNTL TRKLKELGMD
TADDESEEEA LEN
//
