AMIC_PSEAE
ID AMIC_PSEAE Reviewed; 385 AA.
AC P27017;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Aliphatic amidase expression-regulating protein;
GN Name=amiC; OrderedLocusNames=PA3364;
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], AND PROTEIN SEQUENCE OF 2-19.
RC STRAIN=PAC;
RX PubMed=1907262; DOI=10.1128/jb.173.16.4914-4921.1991;
RA Wilson S.A., Drew R.E.;
RT "Cloning and DNA sequence of amiC, a new gene regulating expression of the
RT Pseudomonas aeruginosa aliphatic amidase, and purification of the amiC
RT product.";
RL J. Bacteriol. 173:4914-4921(1991).
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 CRYSTALLIZATION.
RX PubMed=1762155; DOI=10.1016/0022-2836(91)90579-u;
RA Wilson S.A., Chayen N.E., Hemmings A.M., Drew R.E., Pearl L.H.;
RT "Crystallization of and preliminary X-ray data for the negative regulator
RT (AmiC) of the amidase operon of Pseudomonas aeruginosa.";
RL J. Mol. Biol. 222:869-871(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 27-28.
RX PubMed=7813419; DOI=10.1002/j.1460-2075.1994.tb06924.x;
RA Pearl L.H., O'Hara B.P., Drew R.E., Wilson S.A.;
RT "Crystal structure of AmiC: the controller of transcription antitermination
RT in the amidase operon of Pseudomonas aeruginosa.";
RL EMBO J. 13:5810-5817(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIR.
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RC STRAIN=PAC1;
RX PubMed=10708652; DOI=10.1093/protein/13.2.129;
RA O'Hara B.P., Wilson S.A., Lee A.W., Roe S.M., Siligardi G., Drew R.E.,
RA Pearl L.H.;
RT "Structural adaptation to selective pressure for altered ligand specificity
RT in the Pseudomonas aeruginosa amide receptor, AmiC.";
RL Protein Eng. 13:129-132(2000).
CC -!- FUNCTION: Negatively regulates the expression of the aliphatic amidase
CC operon. AmiC functions by inhibiting the action of AmiR at the protein
CC level. It exhibits protein kinase activity.
CC -!- SUBUNIT: Homodimer. Forms a complex with AmiR.
CC -!- DOMAIN: Consists of two beta-alpha-beta domains with a central cleft in
CC which the amide binds.
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DR EMBL; X13776; CAA32024.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06752.1; -; Genomic_DNA.
DR PIR; A40359; A40359.
DR PIR; C83226; C83226.
DR RefSeq; NP_252054.1; NC_002516.2.
DR RefSeq; WP_003091751.1; NZ_QZGE01000017.1.
DR PDB; 1PEA; X-ray; 2.10 A; A=1-385.
DR PDB; 1QNL; X-ray; 2.70 A; A=1-375.
DR PDB; 1QO0; X-ray; 2.25 A; A/B=1-380.
DR PDBsum; 1PEA; -.
DR PDBsum; 1QNL; -.
DR PDBsum; 1QO0; -.
DR AlphaFoldDB; P27017; -.
DR SMR; P27017; -.
DR IntAct; P27017; 1.
DR STRING; 287.DR97_4563; -.
DR DrugBank; DB02736; Acetamide.
DR DrugBank; DB02121; Butyramide.
DR PaxDb; P27017; -.
DR PRIDE; P27017; -.
DR EnsemblBacteria; AAG06752; AAG06752; PA3364.
DR GeneID; 877798; -.
DR KEGG; pae:PA3364; -.
DR PATRIC; fig|208964.12.peg.3523; -.
DR PseudoCAP; PA3364; -.
DR HOGENOM; CLU_027128_1_1_6; -.
DR InParanoid; P27017; -.
DR OMA; YPYESNR; -.
DR PhylomeDB; P27017; -.
DR BioCyc; PAER208964:G1FZ6-3428-MON; -.
DR EvolutionaryTrace; P27017; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0033218; F:amide binding; IDA:PseudoCAP.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; IEA:InterPro.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IDA:PseudoCAP.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0034251; P:regulation of cellular amide catabolic process; IDA:PseudoCAP.
DR CDD; cd06357; PBP1_AmiC; 1.
DR InterPro; IPR039570; AmiC_PBP1.
DR InterPro; IPR000709; Leu_Ile_Val-bd.
DR InterPro; IPR028082; Peripla_BP_I.
DR PRINTS; PR00337; LEUILEVALBP.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Kinase; Reference proteome;
KW Repressor; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1907262"
FT CHAIN 2..385
FT /note="Aliphatic amidase expression-regulating protein"
FT /id="PRO_0000064581"
FT VARIANT 106
FT /note="T -> N (in strain: PAC181; butyramide inducible
FT phenotype)"
FT CONFLICT 27..28
FT /note="QR -> HA (in Ref. 1; CAA32024)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="V -> L (in Ref. 1; CAA32024)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="A -> P (in Ref. 1; CAA32024)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="S -> N (in Ref. 1; CAA32024)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="C -> D (in Ref. 1; CAA32024)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="A -> P (in Ref. 1; CAA32024)"
FT /evidence="ECO:0000305"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 21..39
FT /evidence="ECO:0007829|PDB:1PEA"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:1PEA"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 284..303
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:1PEA"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:1PEA"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:1PEA"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:1QO0"
SQ SEQUENCE 385 AA; 42807 MW; 33924B6C36017B79 CRC64;
MGSHQERPLI GLLFSETGVT ADIERSQRYG ALLAVEQLNR EGGVGGRPIE TLSQDPGGDP
DRYRLCAEDF IRNRGVRFLV GCYMSHTRKA VMPVVERADA LLCYPTPYEG FEYSPNIVYG
GPAPNQNSAP LAAYLIRHYG ERVVFIGSDY IYPRESNHVM RHLYRQHGGT VLEEIYIPLY
PSDDDVQRAV ERIYQARADV VFSTVVGTGT AELYRAIARR YGDGRRPPIA SLTTSEAEVA
KMESDVAEGQ VVVAPYFSSI DTAASRAFVQ ACHGFFPENA TITAWAEAAY WQTLLLGRAA
QAAGSWRVED VQRHLYDICI DAPQGPVRVE RQNNHSRLSS RIAEIDARGV FQVRWQSPEP
IRPDPYVVVH NLDDWSASMG GGALP
