YOAM_BACSU
ID YOAM_BACSU Reviewed; 227 AA.
AC O34906; Q796F3;
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 YoaM;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8R1M0};
GN Name=yoaM; OrderedLocusNames=BSU18660;
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).
RN [3]
RP IDENTIFICATION.
RX PubMed=23945014; DOI=10.1186/1745-6150-8-20;
RA Aravind L., Anand S., Iyer L.M.;
RT "Novel autoproteolytic and DNA-damage sensing components in the bacterial
RT SOS response and oxidized methylcytosine-induced eukaryotic DNA
RT demethylation systems.";
RL Biol. Direct 8:20-20(2013).
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; AAB84423.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13758.1; -; Genomic_DNA.
DR PIR; F69896; F69896.
DR RefSeq; NP_389747.1; NC_000964.3.
DR RefSeq; WP_004399422.1; NZ_CP053102.1.
DR AlphaFoldDB; O34906; -.
DR SMR; O34906; -.
DR STRING; 224308.BSU18660; -.
DR PaxDb; O34906; -.
DR PRIDE; O34906; -.
DR EnsemblBacteria; CAB13758; CAB13758; BSU_18660.
DR GeneID; 940112; -.
DR KEGG; bsu:BSU18660; -.
DR PATRIC; fig|224308.179.peg.2034; -.
DR eggNOG; COG2135; Bacteria.
DR InParanoid; O34906; -.
DR OMA; WQLTATI; -.
DR PhylomeDB; O34906; -.
DR BioCyc; BSUB:BSU18660-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..227
FT /note="Abasic site processing protein YoaM"
FT /id="PRO_0000164401"
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 227 AA; 26233 MW; 9F16195875E1C36D CRC64;
MCGRFTLYSA FDDIIDQFDI DQFFPKGEYQ PSYNVAPSQN ILAIINDGSN NRLGKLRWGL
IPPWAKDEKI GYKMINARAE TITEKPAFRR PLVSKRCIIP ADSFYEWKRL DSKTKIPMRI
KLKSSALFAF AGLYEKWSTH QGYPLYTCTI ITTEPNEFMK DIHDRMPVIL AHDHEKEWLN
PKNTSPDYLQ SLLLPYDADD MEAYQVSSLV NSPKNNSAEL LDAENHM
