YOQW_BPSPB
ID YOQW_BPSPB Reviewed; 224 AA.
AC O64131;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=SOS response-associated protein yoqW;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8R1M0};
GN Name=yoqW; OrderedLocusNames=SPBc2p119;
OS Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Spbetavirus.
OX NCBI_TaxID=66797;
OH NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10376821; DOI=10.1099/13500872-145-5-1055;
RA Lazarevic V., Duesterhoeft A., Soldo B., Hilbert H., Mauel C., Karamata D.;
RT "Nucleotide sequence of the Bacillus subtilis temperate bacteriophage
RT SPbetac2.";
RL Microbiology 145:1055-1067(1999).
CC -!- FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA)
CC required to preserve genome integrity by promoting error-free repair of
CC abasic sites. Recognizes and binds abasic sites in ssDNA at replication
CC forks and chemically modifies the lesion by forming a covalent cross-
CC link with DNA: forms a stable thiazolidine linkage between a ring-
CC opened abasic site and the alpha-amino and sulfhydryl substituents of
CC its N-terminal catalytic cysteine residue (By similarity). May act as a
CC protease: mediates autocatalytic processing of its N-terminal
CC methionine in order to expose the catalytic cysteine (By similarity).
CC {ECO:0000250|UniProtKB:P76318, ECO:0000250|UniProtKB:Q8R1M0}.
CC -!- DOMAIN: Glu-106 is involved in sensing abasic sites in single-stranded
CC DNA (ssDNA). His-163 stabilizes the abasic sites by forming a hydrogen
CC bond with the O4' hydroxyl group. {ECO:0000250|UniProtKB:P76318}.
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {ECO:0000305}.
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DR EMBL; AF020713; AAC13091.1; -; Genomic_DNA.
DR PIR; T12882; T12882.
DR RefSeq; NP_046670.1; NC_001884.1.
DR SMR; O64131; -.
DR GeneID; 1261483; -.
DR KEGG; vg:1261483; -.
DR Proteomes; UP000009091; Genome.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0018142; P:protein-DNA covalent cross-linking; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1680.10; -; 1.
DR InterPro; IPR003738; SRAP.
DR InterPro; IPR036590; SRAP-like.
DR PANTHER; PTHR13604; PTHR13604; 1.
DR Pfam; PF02586; SRAP; 1.
DR SUPFAM; SSF143081; SSF143081; 1.
PE 3: Inferred from homology;
KW Covalent protein-DNA linkage; DNA damage; DNA-binding; Hydrolase; Protease;
KW Reference proteome; SOS response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8R1M0"
FT CHAIN 2..224
FT /note="SOS response-associated protein yoqW"
FT /id="PRO_0000164404"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96FZ2"
FT SITE 106
FT /note="Required for sensing abasic sites"
FT /evidence="ECO:0000250|UniProtKB:P76318"
FT SITE 163
FT /note="Required to stabilize abasic sites"
FT /evidence="ECO:0000250|UniProtKB:P76318"
FT MOD_RES 2
FT /note="Thiazolidine linkage to a ring-opened DNA abasic
FT site"
FT /evidence="ECO:0000250|UniProtKB:P76318"
SQ SEQUENCE 224 AA; 25949 MW; E2234CC340C79B03 CRC64;
MCGRFTLFSE FDDIIEQFNI DQFLPEGEYH PSYNVAPSQN ILTIINDGSN NRLGKLRWGL
IPPWAKDEKI GYKMINARAE TLSEKPSFRK PLVSKRCIIP ADSFYEWKRL DPKTKIPMRI
KLKSSNLFAF AGLYEKWNTP EGNPLYTCTI ITTKPNELME DIHDRMPVIL TDENEKEWLN
PKNTDPDYLQ SLLQPYDADD MEAYQVSSLV NSPKNNSPEL IESH
