ID A0A140DRB6_9FIRM Unreviewed; 939 AA.
AC A0A140DRB6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-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=AALO17_00590 {ECO:0000313|EMBL:AMK53193.1}, BO223_11445
GN {ECO:0000313|EMBL:OLU43634.1};
OS Faecalibaculum rodentium.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalibaculum.
OX NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK53193.1, ECO:0000313|Proteomes:UP000069771};
RN [1] {ECO:0000313|EMBL:AMK53193.1, ECO:0000313|Proteomes:UP000069771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alo17 {ECO:0000313|EMBL:AMK53193.1,
RC ECO:0000313|Proteomes:UP000069771};
RX PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA Lim S., Chang D.H., Ahn S., Kim B.C.;
RT "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT C57BL/6J laboratory mouse feces.";
RL Gut Pathog. 8:3-3(2016).
RN [2] {ECO:0000313|EMBL:OLU43634.1, ECO:0000313|Proteomes:UP000186758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-K8 {ECO:0000313|EMBL:OLU43634.1,
RC ECO:0000313|Proteomes:UP000186758};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00205}.
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DR EMBL; CP011391; AMK53193.1; -; Genomic_DNA.
DR EMBL; MPJZ01000097; OLU43634.1; -; Genomic_DNA.
DR RefSeq; WP_067554020.1; NZ_MPJZ01000097.1.
DR AlphaFoldDB; A0A140DRB6; -.
DR STRING; 1702221.AALO17_00590; -.
DR GeneID; 78476984; -.
DR KEGG; fro:AALO17_00590; -.
DR PATRIC; fig|1702221.3.peg.58; -.
DR OrthoDB; 9809851at2; -.
DR Proteomes; UP000069771; Chromosome.
DR Proteomes; UP000186758; 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: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; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
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};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW Rule:MF_00205};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00205};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00205}; Reference proteome {ECO:0000313|Proteomes:UP000069771};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW SOS response {ECO:0000256|HAMAP-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 324..591
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 604..933
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 249..276
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT ZN_FING 736..762
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 637..644
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 939 AA; 104298 MW; 590BD7D039082972 CRC64;
MENTIKIRGA RENNLKNIDL DIPRDKLVIM TGVSGSGKTS LAFDTIYAEG QRRYMESLSA
YARQFLGNSE KPDVDQIDGL SPAIAIDQKT TSNNPRSTVG TVTEIYDYLR LLYARIGIPY
CPEHGEPIQG MTISEMVDQM MALPDRTRTT IMAPIVRGKK GTFKETFEKL IKDGFIRARV
DGEIVYLEEQ GPLNKNQKHN IDVVVDRIIK SDNRSRFYDS IETAVNLADG MVDVLADDKE
FLLSANYACK ICGFTVPKLE PKLFSFNAPL GACHHCKGLG ITQSVDMDLL IPDRSLSIRQ
GGIRYLKNIV DTENLEWQKM YALIRHYDID MDVPIRDIPK EKLDRILYGS LEPIGYTLYS
RSGSVTEKND MIEGVIPLIE RRFMETNSSW NREWYGSFIS DQTCEECHGA RLDEKVLAVR
VGGKNIYEWT QMSVDEAIEF MKNLQLTDTE KKVSELITKE IRSRLEFLHN VGLTYLTLNR
LAATLSGGEA QRIRLATQIG SRLTGVMYVL DEPSIGLHQR DNDKLIGTMK EMRDLGNTLI
VVEHDEDTMR ASDYIVDVGP GAGIHGGEII KAGTPEEVMA CPDSVTGQYL SGKRSIPVPV
KRRKGNGNTL KIVKATQNNL KGVNATIRLG TLTVVTGVSG SGKSSLVTEV LTKGVEHALG
KLRVKPGACR EIQGLENIDK LVVIGQEPIG RTPRSNPATY TGVFDDIRDL FAQTREAKLL
GYDKGRFSFN VKGGRCESCQ GDGIKRISMH FLPDVYVPCD ACHGKRYNEE TLQVKYKDKT
IADVLDMTVE EAVVFFDGIS RIRHKLQTLK DVGLSYIKLG QSATTLSGGE AQRVKLASEL
QKKPTGKTLF VLDEPTTGLH SADVEKLIEV LQRLVDNGDT VLVIEHNLDV IKNADQIIDI
GPEGGDAGGR IVAAGTPEQV AKVPESWTGQ YLKPLLERK
//
