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Protein

Spermidine/spermine N(1)-acetyltransferase

Gene

paiA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the protection against polyamine toxicity by regulating their concentration. Also could be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It possesses N1-acetyltransferase activity toward polyamine substrates including spermidine, spermine, aminopropylcadaverine, norspermidine, homospermidine, N(8)-acetylspermidine, diaminopropane and agmatine.2 Publications

Catalytic activityi

Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.1 Publication

Kineticsi

Kcat is 21.9 min(-1) for acetyltransferase activity with AcCoA as substrate (at pH 9 and 37 degrees Celius). Kcat is 19.1 min(-1) for acetyltransferase activity with spermine as substrate (at pH 9 and 37 degrees Celius). Kcat is 7.1 min(-1) for acetyltransferase activity with N(1)-acetylspermine as substrate (at pH 9 and 37 degrees Celius). Kcat is 6.1 min(-1) for acetyltransferase activity with aminopropylcadaverine as substrate (at pH 9 and 37 degrees Celius). Kcat is 5.2 min(-1) for acetyltransferase activity with spermidine as substrate (at pH 9 and 37 degrees Celius).1 Publication

  1. KM=31 µM for AcCoA (at pH 9 and 37 degrees Celsius)1 Publication
  2. KM=76 µM for spermine (at pH 9 and 37 degrees Celsius)1 Publication
  3. KM=295 µM for N(1)-acetylspermine (at pH 9 and 37 degrees Celsius)1 Publication
  4. KM=323 µM for spermidine (at pH 9 and 37 degrees Celsius)1 Publication
  5. KM=410 µM for aminopropylcadaverine (at pH 9 and 37 degrees Celsius)1 Publication
  1. Vmax=550 nmol/min/mg enzyme with AcCoA as substrate (at pH 9 and 37 degrees Celsius)1 Publication
  2. Vmax=481 nmol/min/mg enzyme with spermine as substrate (at pH 9 and 37 degrees Celsius)1 Publication
  3. Vmax=178 nmol/min/mg enzyme with N(1)-acetylspermine as substrate (at pH 9 and 37 degrees Celsius)1 Publication
  4. Vmax=154 nmol/min/mg enzyme with aminopropylcadaverine as substrate (at pH 9 and 37 degrees Celsius)1 Publication
  5. Vmax=130 nmol/min/mg enzyme with spermidine as substrate (at pH 9 and 37 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei142 – 1421May have an important role in the acetylation of the polyamine1 Publication
Binding sitei144 – 1441Acetyl-CoA1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU32150-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Spermidine/spermine N(1)-acetyltransferase1 Publication
Short name:
SSAT1 Publication
Alternative name(s):
Protease synthase and sporulation negative regulatory protein PAI 11 Publication
Spermidine N(1)-acetyltransferase1 Publication (EC:2.3.1.571 Publication)
Short name:
SAT1 Publication
Gene namesi
Name:paiA1 Publication
Ordered Locus Names:BSU32150
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene display release of repression of protease synthesis and sporulation in glucose-enriched medium.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 172171Spermidine/spermine N(1)-acetyltransferasePRO_0000058175Add
BLAST

Proteomic databases

PaxDbiP21340.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017451.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi10 – 123Combined sources
Helixi13 – 2816Combined sources
Helixi34 – 4411Combined sources
Helixi47 – 559Combined sources
Beta strandi59 – 668Combined sources
Beta strandi69 – 7810Combined sources
Helixi79 – 813Combined sources
Beta strandi82 – 843Combined sources
Beta strandi90 – 989Combined sources
Helixi100 – 1023Combined sources
Beta strandi104 – 1063Combined sources
Helixi107 – 12115Combined sources
Beta strandi125 – 1328Combined sources
Helixi136 – 1449Combined sources
Beta strandi148 – 15710Combined sources
Beta strandi160 – 17011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TIQX-ray1.90A/B1-172[»]
ProteinModelPortaliP21340.
SMRiP21340. Positions 2-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21340.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 172170N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 983Acetyl-CoA-binding1 Publication
Regioni105 – 1095Acetyl-CoA-binding1 Publication
Regioni135 – 1373Acetyl-CoA-binding1 Publication

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG41090PH. Bacteria.
COG0454. LUCA.
HOGENOMiHOG000078532.
InParanoidiP21340.
OMAiVWEKNEN.
OrthoDBiEOG6XT00Q.
PhylomeDBiP21340.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21340-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVKMKKCSR EDLQTLQQLS IETFNDTFKE QNSPENMKAY LESAFNTEQL
60 70 80 90 100
EKELSNMSSQ FFFIYFDHEI AGYVKVNIDD AQSEEMGAES LEIERIYIKN
110 120 130 140 150
SFQKHGLGKH LLNKAIEIAL ERNKKNIWLG VWEKNENAIA FYKKMGFVQT
160 170
GAHSFYMGDE EQTDLIMAKT LI
Length:172
Mass (Da):20,015
Last modified:January 23, 2007 - v3
Checksum:i391756FDD984B891
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271T → I in AAA22638 (PubMed:2108124).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36471 Genomic DNA. Translation: AAA22638.1.
AL009126 Genomic DNA. Translation: CAB15205.1.
PIRiA35145.
RefSeqiNP_391095.1. NC_000964.3.
WP_003244000.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15205; CAB15205; BSU32150.
GeneIDi937204.
KEGGibsu:BSU32150.
PATRICi18978402. VBIBacSub10457_3364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36471 Genomic DNA. Translation: AAA22638.1.
AL009126 Genomic DNA. Translation: CAB15205.1.
PIRiA35145.
RefSeqiNP_391095.1. NC_000964.3.
WP_003244000.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TIQX-ray1.90A/B1-172[»]
ProteinModelPortaliP21340.
SMRiP21340. Positions 2-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017451.

Proteomic databases

PaxDbiP21340.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15205; CAB15205; BSU32150.
GeneIDi937204.
KEGGibsu:BSU32150.
PATRICi18978402. VBIBacSub10457_3364.

Phylogenomic databases

eggNOGiENOG41090PH. Bacteria.
COG0454. LUCA.
HOGENOMiHOG000078532.
InParanoidiP21340.
OMAiVWEKNEN.
OrthoDBiEOG6XT00Q.
PhylomeDBiP21340.

Enzyme and pathway databases

BioCyciBSUB:BSU32150-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP21340.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel Bacillus subtilis gene involved in negative control of sporulation and degradative-enzyme production."
    Honjo M., Nakayama A., Fukazawa K., Kawamura K., Ando K., Hori M., Furutani Y.
    J. Bacteriol. 172:1783-1790(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT.
    Strain: 168 / DB104.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase."
    Forouhar F., Lee I.-S., Vujcic J., Vujcic S., Shen J., Vorobiev S.M., Xiao R., Acton T.B., Montelione G.T., Porter C.W., Tong L.
    J. Biol. Chem. 280:40328-40336(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT.

Entry informationi

Entry nameiPAIA_BACSU
AccessioniPrimary (citable) accession number: P21340
Secondary accession number(s): O32112
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.