ID   YOBE_BACSU              Reviewed;         219 AA.
AC   O34915; Q796E6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Abasic site processing protein YobE;
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:Q8R1M0};
GN   Name=yobE; OrderedLocusNames=BSU18880;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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).
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; AF027868; AAB84428.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13780.1; -; Genomic_DNA.
DR   PIR; E69898; E69898.
DR   RefSeq; NP_389769.1; NC_000964.3.
DR   RefSeq; WP_004399318.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34915; -.
DR   SMR; O34915; -.
DR   PaxDb; O34915; -.
DR   PRIDE; O34915; -.
DR   EnsemblBacteria; CAB13780; CAB13780; BSU_18880.
DR   GeneID; 939611; -.
DR   KEGG; bsu:BSU18880; -.
DR   PATRIC; fig|224308.179.peg.2059; -.
DR   eggNOG; COG2135; Bacteria.
DR   InParanoid; O34915; -.
DR   OMA; MCFHSKQ; -.
DR   PhylomeDB; O34915; -.
DR   BioCyc; BSUB:BSU18880-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..219
FT                   /note="Abasic site processing protein YobE"
FT                   /id="PRO_0000164402"
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   219 AA;  25241 MW;  95B1DF357C4188CF CRC64;
     MCGKFTLFSE FDDIIEQFNI DQFLPEGEYH PSYNVAPSQN ILTIINDGSN NRLGKLRWGL
     IPPCAKDEKI GYKMINARAE TLAEKPSFRK PLGSKRCIIP ADSFYEWKRL DPKTKIPMRI
     KLKSSNLFAF AGLYEKWNTL EGNLLYTCTI ITIKPSELME DIHDRMPVIL TDENKKEWLN
     PKNTDPDYLQ SLLLPYDADD MEAYQVSSLV NSPELIESH