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Protein

Stage IV sporulation protein A

Gene

spoIVA

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

Functioni

ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.5 Publications

Miscellaneous

Present in an increased level in yabG mutant spores.

Catalytic activityi

ATP + H2O = ADP + phosphate.2 Publications

Kineticsi

The turnover rate is 2.7 pmol/min/pmol of SpoIVA at Vmax (PubMed:18691972). The turnover rate is 1.0 pmol/min/pmol of SpoIVA at Vmax (PubMed:23267091).2 Publications
  1. KM=412 µM for ATP2 Publications

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi24 – 31ATPCurated8

    GO - Molecular functioni

    • ATPase activity Source: UniProtKB
    • ATP binding Source: UniProtKB

    GO - Biological processi

    • peptidoglycan metabolic process Source: UniProtKB
    • protein complex oligomerization Source: UniProtKB
    • protein polymerization Source: UniProtKB
    • spore germination Source: UniProtKB
    • spore wall assembly Source: UniProtKB
    • spore wall biogenesis Source: UniProtKB
    • sporulation Source: UniProtKB
    • sporulation resulting in formation of a cellular spore Source: UniProtKB

    Keywordsi

    Molecular functionHydrolase
    Biological processSporulation
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU22800-MONOMER

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stage IV sporulation protein A (EC:3.6.1.3)
    Alternative name(s):
    Coat morphogenetic protein SpoIVA
    Gene namesi
    Name:spoIVA
    Synonyms:spoVP
    Ordered Locus Names:BSU22800
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB-SubCell
    • endospore cortex Source: UniProtKB
    • endospore-forming forespore Source: UniProtKB
    • spore wall Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Forespores lack a well-defined cortex, and the coat is present as swirls in the mother cell compartment of the sporangia rather than having been deposited around the forespore protoplasts. According to PubMed:18691972, unable to sporulate.3 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi30K → A: 20-fold reduction in sporulation efficiency. Largely enriched at the forespore periphery, although some localization to the cytosol. Binding of ATP reduced over 23-fold. Leads to diminished ATP hydrolysis. 1 Publication1
    Mutagenesisi30K → E: Mislocalized to the mother cell cytosol. Misassembles the spore coat. Mislocalizes CotE but not SpoVM. Does not multimerize. Almost complete block in spore formation. 1 Publication1
    Mutagenesisi59L → P: Spores form largely normal coats and possess at least some cortex, but cannot remain dehydrated after mother cell lysis. Abnormal synthesis and an insufficient level of spore peptidoglycan, which contains amidated diaminopimelic acid, which is normally found only in vegetative cell peptidoglycan. Defective in germination; when associated with P-256. 1 Publication1
    Mutagenesisi69M → L: Altered cortex and coat formation; when associated with S-230. 1 Publication1
    Mutagenesisi70T → A: 500-fold decrease in sporulation efficiency. 5-log decrease in sporulation efficiency; no ATPase activity, but no change in ATP-binding ability; unable to polymerize and fails to promote coat assembly; when associated with A-71. 1 Publication1
    Mutagenesisi71T → A: Does not abrogate sporulation. 5-log decrease in sporulation efficiency; no ATPase activity, but no change in ATP-binding ability; unable to polymerize and fails to promote coat assembly; when associated with A-70. 1 Publication1
    Mutagenesisi97D → A: Completely abolished sporulation efficiency. No ATPase activity, but no change in ATP-binding ability. Unable to polymerize and fails to promote coat assembly;. 1 Publication1
    Mutagenesisi98C → S: Defective in germination; when associated with N-283. 1 Publication1
    Mutagenesisi189S → K: Unable to sporulate. 1 Publication1
    Mutagenesisi210I → A: Defective in germination; when associated with V-367 and R-383. 1 Publication1
    Mutagenesisi210I → M: Altered cortex and coat formation; when associated with V-367 and R-383. 1 Publication1
    Mutagenesisi230R → S: Altered cortex and coat formation; when associated with L-69. 1 Publication1
    Mutagenesisi241V → G: Altered cortex and coat formation. 1 Publication1
    Mutagenesisi256H → P: Defective in germination; when associated with P-59. 1 Publication1
    Mutagenesisi283V → N: Defective in germination; when associated with S-98. 1 Publication1
    Mutagenesisi367I → V: Defective in germination; when associated with A-210 and R-383. Altered cortex and coat formation; when associated with M-210 and R-383. 1 Publication1
    Mutagenesisi383I → R: Defective in germination; when associated with A-210 and V-367. Altered cortex and coat formation; when associated with M-210 and R-383. 1 Publication1
    Mutagenesisi393L → P: Altered cortex and coat formation. Possesses swirls of coat in the mother cell cytoplasm and does not possess a cortex. 1 Publication1
    Mutagenesisi400I → P: Altered cortex and coat formation, affects localization to the forespore; when associated with R-457 and V-418. 1 Publication1
    Mutagenesisi416G → R: Altered cortex and coat formation. 1 Publication1
    Mutagenesisi418E → V: Altered cortex and coat formation, affects localization to the forespore; when associated with P-400 and R-457. 1 Publication1
    Mutagenesisi453V → G: Altered cortex and coat formation, affects localization to the forespore. 1 Publication1
    Mutagenesisi457I → R: Altered cortex and coat formation, affects localization to the forespore; when associated with P-400 and V-418. 1 Publication1
    Mutagenesisi486G → V: Suppressor mutation that reverses the mislocalization and sporulation defect of the A-6 mutation in SpoVM. Causes little impairment of sporulation. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000720731 – 492Stage IV sporulation protein AAdd BLAST492

    Post-translational modificationi

    Seems to be cleaved by the YabG protease.1 Publication

    Proteomic databases

    PaxDbiP35149
    PRIDEiP35149

    Expressioni

    Developmental stagei

    Expressed soon after the formation of the asymmetric septum during sporulation. Expression commences about 2 hours after the onset of sporulation. Assembly around the developing forespore commences at the time of polar division and seems to continue after engulfment of the forespore is complete. Remains present throughout the late stages of morphogenesis and during this accumulation process preferentially collects on the mother cell side of the engulfed forespore, but eventually is deposited equally all around the forespore.3 Publications

    Interactioni

    Subunit structurei

    Polymerizes to self-assemble into static filaments. ATP hydrolysis is required by every subunit for incorporation into the growing polymer by inducing a conformational change that drives polymerization of a nucleotide-free filament. Polymerization requires a critical concentration of the protein and only occurs after it is localized to the surface of the developing spore. Interacts (via extreme C-terminus Gly-486) with SpoVM (via Ile-6). Interacts (via full-length) with SpoVID (via C-terminus 499-575 AA). Interacts with SafA.5 Publications

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100012526

    Structurei

    3D structure databases

    ProteinModelPortaliP35149
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi24 – 31Walker A motif; involved in ATP-binding and hydrolysis8

    Domaini

    Extreme C-terminal region (AA 487-492) is required for its proper localization into a spherical shell around the developing forespore. N-teminus (AA 1-64) is functionally important although largely dispensable for proper localization.1 Publication

    Phylogenomic databases

    eggNOGiENOG4105DXU Bacteria
    ENOG410XQ51 LUCA
    HOGENOMiHOG000058353
    KOiK06398
    OMAiRMVTTPW
    PhylomeDBiP35149

    Family and domain databases

    InterProiView protein in InterPro
    IPR027417 P-loop_NTPase
    IPR014201 Spore_IV_A
    PfamiView protein in Pfam
    PF09547 Spore_IV_A, 1 hit
    PIRSFiPIRSF007466 SpoIVA, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    TIGRFAMsiTIGR02836 spore_IV_A, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P35149-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEKVDIFKDI AERTGGDIYL GVVGAVRTGK STFIKKFMEL VVLPNISNEA
    60 70 80 90 100
    DRARAQDELP QSAAGKTIMT TEPKFVPNQA MSVHVSDGLD VNIRLVDCVG
    110 120 130 140 150
    YTVPGAKGYE DENGPRMINT PWYEEPIPFH EAAEIGTRKV IQEHSTIGVV
    160 170 180 190 200
    ITTDGTIGDI ARSDYIEAEE RVIEELKEVG KPFIMVINSV RPYHPETEAM
    210 220 230 240 250
    RQDLSEKYDI PVLAMSVESM RESDVLSVLR EALYEFPVLE VNVNLPSWVM
    260 270 280 290 300
    VLKENHWLRE SYQESVKETV KDIKRLRDVD RVVGQFSEFE FIESAGLAGI
    310 320 330 340 350
    ELGQGVAEID LYAPDHLYDQ ILKEVVGVEI RGRDHLLELM QDFAHAKTEY
    360 370 380 390 400
    DQVSDALKMV KQTGYGIAAP ALADMSLDEP EIIRQGSRFG VRLKAVAPSI
    410 420 430 440 450
    HMIKVDVESE FAPIIGTEKQ SEELVRYLMQ DFEDDPLSIW NSDIFGRSLS
    460 470 480 490
    SIVREGIQAK LSLMPENARY KLKETLERII NEGSGGLIAI IL
    Length:492
    Mass (Da):55,175
    Last modified:February 1, 1994 - v1
    Checksum:i29EBA349DD18D12A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M81169 Genomic DNA Translation: AAA22802.1
    M80926 Genomic DNA Translation: AAB59029.1
    AL009126 Genomic DNA Translation: CAB14196.1
    PIRiA41970
    RefSeqiNP_390161.1, NC_000964.3
    WP_003230572.1, NZ_JNCM01000036.1

    Genome annotation databases

    EnsemblBacteriaiCAB14196; CAB14196; BSU22800
    GeneIDi938991
    KEGGibsu:BSU22800
    PATRICifig|224308.179.peg.2485

    Entry informationi

    Entry nameiSP4A_BACSU
    AccessioniPrimary (citable) accession number: P35149
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: May 23, 2018
    This is version 106 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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