AMIR_PSEAE
ID AMIR_PSEAE Reviewed; 196 AA.
AC P10932;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Aliphatic amidase regulator;
GN Name=amiR; OrderedLocusNames=PA3363;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAC433;
RX PubMed=2495988; DOI=10.1016/0014-5793(89)80249-2;
RA Lowe N., Rice P.M., Drew R.E.;
RT "Nucleotide sequence of the aliphatic amidase regulator gene (amiR) of
RT Pseudomonas aeruginosa.";
RL FEBS Lett. 246:39-43(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP CHARACTERIZATION.
RX PubMed=7539417; DOI=10.1128/jb.177.11.3052-3057.1995;
RA Wilson S.A., Drew R.E.;
RT "Transcriptional analysis of the amidase operon from Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 177:3052-3057(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIC.
RC STRAIN=PAC1;
RX PubMed=10508151; DOI=10.1093/emboj/18.19.5175;
RA O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E.,
RA Pearl L.H.;
RT "Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated
RT transcription antitermination complex.";
RL EMBO J. 18:5175-5186(1999).
CC -!- FUNCTION: Positive controlling element of AmiE, the gene for aliphatic
CC amidase. Acts as a transcriptional antitermination factor. It is
CC thought to allow RNA polymerase read through a rho-independent
CC transcription terminator between the AmiE promoter and gene.
CC -!- SUBUNIT: Forms a complex with AmiC.
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DR EMBL; X13776; CAA32023.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06751.1; -; Genomic_DNA.
DR PIR; B83226; B83226.
DR PIR; S03884; S03884.
DR RefSeq; NP_252053.1; NC_002516.2.
DR RefSeq; WP_003113131.1; NZ_QZGE01000017.1.
DR PDB; 1QO0; X-ray; 2.25 A; D/E=1-195.
DR PDBsum; 1QO0; -.
DR AlphaFoldDB; P10932; -.
DR SMR; P10932; -.
DR IntAct; P10932; 1.
DR STRING; 287.DR97_4564; -.
DR PaxDb; P10932; -.
DR DNASU; 880573; -.
DR EnsemblBacteria; AAG06751; AAG06751; PA3363.
DR GeneID; 880573; -.
DR KEGG; pae:PA3363; -.
DR PATRIC; fig|208964.12.peg.3522; -.
DR PseudoCAP; PA3363; -.
DR HOGENOM; CLU_108803_1_0_6; -.
DR OMA; AYENPTF; -.
DR PhylomeDB; P10932; -.
DR BioCyc; PAER208964:G1FZ6-3427-MON; -.
DR EvolutionaryTrace; P10932; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IDA:PseudoCAP.
DR GO; GO:0044248; P:cellular catabolic process; IDA:PseudoCAP.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IMP:PseudoCAP.
DR GO; GO:0034251; P:regulation of cellular amide catabolic process; IDA:PseudoCAP.
DR GO; GO:0031564; P:transcription antitermination; IDA:PseudoCAP.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005561; ANTAR.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR008327; Sig_transdc_resp-reg_antiterm.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF03861; ANTAR; 1.
DR PIRSF; PIRSF036382; RR_antiterm; 1.
DR SMART; SM01012; ANTAR; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50921; ANTAR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transcription;
KW Transcription antitermination; Transcription regulation.
FT CHAIN 1..196
FT /note="Aliphatic amidase regulator"
FT /id="PRO_0000064582"
FT DOMAIN 129..190
FT /note="ANTAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00308"
FT CONFLICT 48
FT /note="S -> A (in Ref. 1; CAA32023)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="R -> G (in Ref. 1; CAA32023)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="E -> D (in Ref. 1; CAA32023)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="A -> V (in Ref. 1; CAA32023)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="Y -> H (in Ref. 1; CAA32023)"
FT /evidence="ECO:0000305"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:1QO0"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:1QO0"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1QO0"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:1QO0"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1QO0"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1QO0"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1QO0"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1QO0"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1QO0"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1QO0"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1QO0"
FT HELIX 115..160
FT /evidence="ECO:0007829|PDB:1QO0"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:1QO0"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:1QO0"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:1QO0"
SQ SEQUENCE 196 AA; 21903 MW; 306A4F30E8E4C6C0 CRC64;
MSANSLLGSL RELQVLVLNP PGEVSDALVL QLIRIGCSVR QCWPPPESFD VPVDVVFTSI
FQNRHHDEIA ALLAAGTPRT TLVALVEYES PAVLSQIIEL ECHGVITQPL DAHRVLPVLV
SARRISEEMA KLKQKTEQLQ ERIAGQARIN QAKALLMQRH GWDEREAHQY LSREAMKRRE
PILKIAQELL GNEPSA
