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Database: UniProt
Entry: A0A2I5T434_SERS3
LinkDB: A0A2I5T434_SERS3
Original site: A0A2I5T434_SERS3 
ID   A0A2I5T434_SERS3        Unreviewed;       631 AA.
AC   A0A2I5T434;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=DNA mismatch repair protein MutL {ECO:0000256|ARBA:ARBA00021975, ECO:0000256|HAMAP-Rule:MF_00149};
GN   Name=mutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN   ORFNames=CWC46_05550 {ECO:0000313|EMBL:AUG99323.1}, Ser39006_005555
GN   {ECO:0000313|EMBL:AUH03641.1};
OS   Serratia sp. (strain ATCC 39006).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=104623 {ECO:0000313|EMBL:AUH03641.1, ECO:0000313|Proteomes:UP000017700};
RN   [1] {ECO:0000313|EMBL:AUH03641.1, ECO:0000313|Proteomes:UP000017700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH03641.1}, and ATCC 39006 / SC
RC   11482 {ECO:0000313|Proteomes:UP000017700};
RX   PubMed=24336377; DOI=10.1128/genomeA.01039-13;
RA   Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA   McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA   Brugger K., Brown S.D., Salmond G.P.;
RT   "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT   for analysis of the biosynthesis and regulation of prodigiosin, a
RT   carbapenem, and gas vesicles.";
RL   Genome Announc. 1:E01039-E01039(2013).
RN   [2] {ECO:0000313|EMBL:AUH03641.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH03641.1};
RA   Wang G., Yang Y., Su Y.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AUG99323.1, ECO:0000313|Proteomes:UP000233778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUG99323.1,
RC   ECO:0000313|Proteomes:UP000233778};
RA   Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA   Fineran P.C.;
RT   "Complete genome sequence of Serratia sp. ATCC 39006 LacA.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AUH03641.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH03641.1};
RA   Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA   Fineran P.C.;
RT   "Complete genome sequence of Serratia sp. ATCC 39006.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is involved in the repair of mismatches in DNA.
CC       It is required for dam-dependent methyl-directed DNA mismatch repair.
CC       May act as a 'molecular matchmaker', a protein that promotes the
CC       formation of a stable complex between two or more DNA-binding proteins
CC       in an ATP-dependent manner without itself being part of a final
CC       effector complex. {ECO:0000256|HAMAP-Rule:MF_00149}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082, ECO:0000256|HAMAP-Rule:MF_00149}.
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DR   EMBL; CP025085; AUG99323.1; -; Genomic_DNA.
DR   EMBL; CP025084; AUH03641.1; -; Genomic_DNA.
DR   RefSeq; WP_021017252.1; NZ_CP025085.1.
DR   AlphaFoldDB; A0A2I5T434; -.
DR   STRING; 104623.Ser39006_03992; -.
DR   KEGG; sera:Ser39006_005555; -.
DR   KEGG; serq:CWC46_05550; -.
DR   OrthoDB; 9763467at2; -.
DR   Proteomes; UP000017700; Chromosome.
DR   Proteomes; UP000233778; Chromosome.
DR   GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-UniRule.
DR   CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR   CDD; cd03482; MutL_Trans_MutL; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR   Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 1.
DR   HAMAP; MF_00149; DNA_mis_repair; 1.
DR   InterPro; IPR014762; DNA_mismatch_repair_CS.
DR   InterPro; IPR020667; DNA_mismatch_repair_MutL.
DR   InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR002099; MutL/Mlh/PMS.
DR   InterPro; IPR038973; MutL/Mlh/Pms-like.
DR   InterPro; IPR014790; MutL_C.
DR   InterPro; IPR042120; MutL_C_dimsub.
DR   InterPro; IPR042121; MutL_C_regsub.
DR   InterPro; IPR037198; MutL_C_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00585; mutl; 1.
DR   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF12; DNA MISMATCH REPAIR PROTEIN MLH1; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF08676; MutL_C; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SMART; SM00853; MutL_C; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF118116; DNA mismatch repair protein MutL; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00149};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00149}; Endonuclease {ECO:0000313|EMBL:AUH03641.1};
KW   Hydrolase {ECO:0000313|EMBL:AUH03641.1};
KW   Nuclease {ECO:0000313|EMBL:AUH03641.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017700}.
FT   DOMAIN          212..330
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          454..589
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          371..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  70237 MW;  57DAD8212519B80B CRC64;
     MPIQVLPPQL ANQIAAGEVV ERPASVVKEL VENSLDAGAT RIDIDIERGG SKLIRIRDNG
     SGISKEDLTL ALARHATSKI ATLDDLEAII SLGFRGEALA SISSVSRLTL TSRTVQQNEA
     WQAYAEGRDM DVTVKPAAHP VGTTLEVLDL FYNTPARRKF MRAEKTEFTH IDEVVRRIAL
     ARFDIAINLN HNGKLIRQYR AVSDASQYER RLGNICGAAF LQHALAVSWQ HGDLKIHGWV
     ADPAGARQLP EMQYCYVNQR MMRDRLINHA IRQAYQDQLK DEQQPAYVLY LEVDPHQVDV
     NVHPAKHEVR FHQARLVHDF IYQAVMTVLQ QSAAPILPIT EPGVEPTPVW QQENRTASGG
     NHFARTISSS VEKAVSEPAS TTARERQPAP YLSGSGYQKK QGELYQKLLQ PKQPLSGTPG
     SSPVETVLKP PSPAVSQVMS TAPLASNDQG LGRVLTVYPP CYALVEYQQG LAILSLTVAE
     RHLKQAQLTP TTEGLRPQPL LIPQRLTLDK KELSVLSQHQ ALLTQFGIDV AIEQQRATLR
     AVPLPLRQQN LQNLISYLLG YLADYPMAES EQIAVWMAHQ LLSEHENWTH AQAIQLLTEV
     ERLCPQWVRN PPPEFLGVMD IDAAIKALKH D
//
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