PAIA_BACSU
ID PAIA_BACSU Reviewed; 172 AA.
AC P21340; O32112;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Spermidine/spermine N(1)-acetyltransferase {ECO:0000303|PubMed:16210326};
DE Short=SSAT {ECO:0000303|PubMed:16210326};
DE AltName: Full=Protease synthase and sporulation negative regulatory protein PAI 1 {ECO:0000303|PubMed:16210326};
DE AltName: Full=Spermidine N(1)-acetyltransferase {ECO:0000303|PubMed:16210326};
DE Short=SAT {ECO:0000303|PubMed:16210326};
DE EC=2.3.1.57 {ECO:0000269|PubMed:16210326};
GN Name=paiA {ECO:0000303|PubMed:2108124}; OrderedLocusNames=BSU32150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION,
RP DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=168 / DB104;
RX PubMed=2108124; DOI=10.1128/jb.172.4.1783-1790.1990;
RA Honjo M., Nakayama A., Fukazawa K., Kawamura K., Ando K., Hori M.,
RA Furutani Y.;
RT "A novel Bacillus subtilis gene involved in negative control of sporulation
RT and degradative-enzyme production.";
RL J. Bacteriol. 172:1783-1790(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3] {ECO:0007744|PDB:1TIQ}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RX PubMed=16210326; DOI=10.1074/jbc.m505332200;
RA Forouhar F., Lee I.-S., Vujcic J., Vujcic S., Shen J., Vorobiev S.M.,
RA Xiao R., Acton T.B., Montelione G.T., Porter C.W., Tong L.;
RT "Structural and functional evidence for Bacillus subtilis PaiA as a novel
RT N1-spermidine/spermine acetyltransferase.";
RL J. Biol. Chem. 280:40328-40336(2005).
CC -!- FUNCTION: Involved in the protection against polyamine toxicity by
CC regulating their concentration. Could also be involved in the negative
CC control of sporulation as well as production of degradative enzymes
CC such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes
CC the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an
CC acceptor substrate and releases both CoA and the acetylated product. It
CC possesses N1-acetyltransferase activity toward polyamine substrates
CC including spermidine, spermine, aminopropylcadaverine, norspermidine,
CC homospermidine, N(8)-acetylspermidine, diaminopropane and agmatine.
CC {ECO:0000269|PubMed:16210326, ECO:0000269|PubMed:2108124}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-
CC acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116,
CC Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977,
CC ChEBI:CHEBI:70988; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:16210326};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 uM for AcCoA (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16210326};
CC KM=76 uM for spermine (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16210326};
CC KM=295 uM for N(1)-acetylspermine (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16210326};
CC KM=323 uM for spermidine (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16210326};
CC KM=410 uM for aminopropylcadaverine (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16210326};
CC Vmax=550 nmol/min/mg enzyme with AcCoA as substrate (at pH 9 and 37
CC degrees Celsius) {ECO:0000269|PubMed:16210326};
CC Vmax=481 nmol/min/mg enzyme with spermine as substrate (at pH 9 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:16210326};
CC Vmax=178 nmol/min/mg enzyme with N(1)-acetylspermine as substrate (at
CC pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326};
CC Vmax=154 nmol/min/mg enzyme with aminopropylcadaverine as substrate
CC (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326};
CC Vmax=130 nmol/min/mg enzyme with spermidine as substrate (at pH 9 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:16210326};
CC Note=kcat is 21.9 min(-1) for acetyltransferase activity with AcCoA
CC as substrate (at pH 9 and 37 degrees Celsius). kcat is 19.1 min(-1)
CC for acetyltransferase activity with spermine as substrate (at pH 9
CC and 37 degrees Celsius). kcat is 7.1 min(-1) for acetyltransferase
CC activity with N(1)-acetylspermine as substrate (at pH 9 and 37
CC degrees Celsius). kcat is 6.1 min(-1) for acetyltransferase activity
CC with aminopropylcadaverine as substrate (at pH 9 and 37 degrees
CC Celsius). kcat is 5.2 min(-1) for acetyltransferase activity with
CC spermidine as substrate (at pH 9 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:16210326};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16210326,
CC ECO:0000269|PubMed:2108124}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display release of
CC repression of protease synthesis and sporulation in glucose-enriched
CC medium. {ECO:0000269|PubMed:2108124}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; M36471; AAA22638.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15205.1; -; Genomic_DNA.
DR PIR; A35145; A35145.
DR RefSeq; NP_391095.1; NC_000964.3.
DR RefSeq; WP_003244000.1; NZ_JNCM01000033.1.
DR PDB; 1TIQ; X-ray; 1.90 A; A/B=1-172.
DR PDBsum; 1TIQ; -.
DR AlphaFoldDB; P21340; -.
DR SMR; P21340; -.
DR STRING; 224308.BSU32150; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB01992; Coenzyme A.
DR PaxDb; P21340; -.
DR PRIDE; P21340; -.
DR EnsemblBacteria; CAB15205; CAB15205; BSU_32150.
DR GeneID; 937204; -.
DR KEGG; bsu:BSU32150; -.
DR PATRIC; fig|224308.179.peg.3481; -.
DR eggNOG; COG0456; Bacteria.
DR InParanoid; P21340; -.
DR OMA; QFFFVYF; -.
DR PhylomeDB; P21340; -.
DR BioCyc; BSUB:BSU32150-MON; -.
DR EvolutionaryTrace; P21340; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043939; P:negative regulation of sporulation; IMP:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing;
KW Reference proteome; Sporulation; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2108124"
FT CHAIN 2..172
FT /note="Spermidine/spermine N(1)-acetyltransferase"
FT /id="PRO_0000058175"
FT DOMAIN 3..172
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 96..98
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:16210326"
FT BINDING 105..109
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:16210326"
FT BINDING 135..137
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:16210326"
FT BINDING 144
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:16210326"
FT SITE 142
FT /note="May have an important role in the acetylation of the
FT polyamine"
FT /evidence="ECO:0000305|PubMed:16210326"
FT CONFLICT 27
FT /note="T -> I (in Ref. 1; AAA22638)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1TIQ"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1TIQ"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:1TIQ"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1TIQ"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:1TIQ"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1TIQ"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:1TIQ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1TIQ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1TIQ"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:1TIQ"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1TIQ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1TIQ"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:1TIQ"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1TIQ"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:1TIQ"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:1TIQ"
FT STRAND 160..170
FT /evidence="ECO:0007829|PDB:1TIQ"
SQ SEQUENCE 172 AA; 20015 MW; 391756FDD984B891 CRC64;
MSVKMKKCSR EDLQTLQQLS IETFNDTFKE QNSPENMKAY LESAFNTEQL EKELSNMSSQ
FFFIYFDHEI AGYVKVNIDD AQSEEMGAES LEIERIYIKN SFQKHGLGKH LLNKAIEIAL
ERNKKNIWLG VWEKNENAIA FYKKMGFVQT GAHSFYMGDE EQTDLIMAKT LI
