ID A0A0R1W7B4_9LACO Unreviewed; 949 AA.
AC A0A0R1W7B4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316, ECO:0000256|HAMAP-Rule:MF_00205};
DE Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205};
DE AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156, ECO:0000256|HAMAP-Rule:MF_00205};
GN Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN ORFNames=FD16_GL000162 {ECO:0000313|EMBL:KRM13591.1};
OS Paucilactobacillus suebicus DSM 5007 = KCTC 3549.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM13591.1, ECO:0000313|Proteomes:UP000051820};
RN [1] {ECO:0000313|EMBL:KRM13591.1, ECO:0000313|Proteomes:UP000051820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM13591.1,
RC ECO:0000313|Proteomes:UP000051820};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein.
CC A damage recognition complex composed of 2 UvrA and 2 UvrB subunits
CC scans DNA for abnormalities. When the presence of a lesion has been
CC verified by UvrB, the UvrA molecules dissociate. {ECO:0000256|HAMAP-
CC Rule:MF_00205}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC lesions. {ECO:0000256|HAMAP-Rule:MF_00205}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00205}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000256|ARBA:ARBA00038000, ECO:0000256|HAMAP-Rule:MF_00205}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM13591.1}.
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DR EMBL; AZGF01000001; KRM13591.1; -; Genomic_DNA.
DR RefSeq; WP_010622913.1; NZ_BACO01000065.1.
DR AlphaFoldDB; A0A0R1W7B4; -.
DR STRING; 1423807.FD16_GL000162; -.
DR PATRIC; fig|1423807.3.peg.163; -.
DR eggNOG; COG0178; Bacteria.
DR OrthoDB; 9809851at2; -.
DR Proteomes; UP000051820; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd03270; ABC_UvrA_I; 1.
DR CDD; cd03271; ABC_UvrA_II; 1.
DR Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004602; UvrA.
DR InterPro; IPR041552; UvrA_DNA-bd.
DR InterPro; IPR041102; UvrA_inter.
DR NCBIfam; TIGR00630; uvra; 1.
DR PANTHER; PTHR43152; UVRABC SYSTEM PROTEIN A; 1.
DR PANTHER; PTHR43152:SF3; UVRABC SYSTEM PROTEIN A; 1.
DR Pfam; PF17755; UvrA_DNA-bind; 1.
DR Pfam; PF17760; UvrA_inter; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00205};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00205};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00205};
KW DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW Rule:MF_00205};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00205};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00205}; Endonuclease {ECO:0000313|EMBL:KRM13591.1};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW Rule:MF_00205}; Hydrolase {ECO:0000313|EMBL:KRM13591.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00205}; Nuclease {ECO:0000313|EMBL:KRM13591.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00205};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00205};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00205};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_00205}.
FT DOMAIN 599..936
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 253..280
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT ZN_FING 739..765
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 640..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 949 AA; 104980 MW; 4BA35D112FA2104E CRC64;
MATNDKIKIH GARAHNLKNI DVTIPKNKLV VVTGLSGSGK SSLAFDTLYA EGQRRYVESL
SAYARQFLGQ MDKPDVDSID GLSPAISIDQ KTTSKNPRST VGTVTEINDY LRLLWARVGT
PICPNDGTPI TSQSPEQMVD RVLNLPERTK LQILSPIVRD KKGGQKKTFE KVKREGFIRV
RVDDETYDID EVPELNKNLK HSVDVVIDRI VVKDGIRSRL FDSFEAALRL SDGYATADII
GGEPIAFSEQ YACPICGFTV GEMEPRLFSF NAPLGACPEC EGLGVKLEVD EDLVVPDRTK
TLAEGALLPW NPISSQYYPE MLKQFCDQNE IDMDIPFEDL PAKQQKIILY GNGDTLFHFH
YENEFGGVRD VDAKFEGVLN NVERRYHETN SDFTRDQMRK YMTELTCQSC HGYRLNRQAL
SVKVDGQHIG EVSDKPVSDE LPFFRSLTLS EQNEVIARPI IKEICDRLEF LQNVGLDYLT
LSRSARTLSG GEAQRIRLAT QIGSNLSGVM YILDEPSIGL HQRDNDRLIA SLKKMRDLGN
TLIIVEHDED TMRAADYIVD IGPGAGDNGG EVMAAGTPKQ VSRSRKSLTG QYLSGKKFIE
VPDSRRVGNG KKLTLTGAAE NNLKDITVDF PLGKFVAVTG VSGSGKSTLV NSVLKRVLAQ
KLNHNSEKPG KYKTVRGINN IEKVIDIDQA PIGRTPRSNP ATYTGVFDDI RGLFAQTNAA
KMRGYSKGRF SFNIKGGRCE ACHGDGILKI EMNFLPDVYV PCEVCHGKRY NSETLEVEYK
GKNIADVLDM TVEEALQFFS AIPKITRKLQ TIVDVGLGYV KMGQPATTLS GGEAQRMKLA
SELHKQSTGK SFYILDEPTT GLHTDDIKRL LDVLQRLVDA GNTVLVIEHN LDVVKSADWL
IDLGPEGGAG GGQVVATGTP EEVAEVKESY TGKYLKPVLV RDKERQVKA
//
