YOQW_BACSU
ID YOQW_BACSU Reviewed; 224 AA.
AC O31916;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Abasic site processing protein YoqW;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8R1M0};
GN Name=yoqW; OrderedLocusNames=BSU20490;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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).
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; AL009126; CAB13941.1; -; Genomic_DNA.
DR RefSeq; NP_389931.1; NC_000964.3.
DR RefSeq; WP_004399300.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O31916; -.
DR SMR; O31916; -.
DR STRING; 224308.BSU20490; -.
DR PaxDb; O31916; -.
DR PRIDE; O31916; -.
DR EnsemblBacteria; CAB13941; CAB13941; BSU_20490.
DR GeneID; 939979; -.
DR KEGG; bsu:BSU20490; -.
DR PATRIC; fig|224308.179.peg.2239; -.
DR eggNOG; COG2135; Bacteria.
DR InParanoid; O31916; -.
DR OMA; FPARYNI; -.
DR PhylomeDB; O31916; -.
DR BioCyc; BSUB:BSU20490-MON; -.
DR Proteomes; UP000001570; Chromosome.
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="Abasic site processing protein YoqW"
FT /id="PRO_0000164403"
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
