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Database: UniProt
Entry: A0A401UX37_9CELL
LinkDB: A0A401UX37_9CELL
Original site: A0A401UX37_9CELL 
ID   A0A401UX37_9CELL        Unreviewed;       952 AA.
AC   A0A401UX37;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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_1 {ECO:0000313|EMBL:GCD19194.1};
GN   Synonyms=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN   ORFNames=CTKZ_07560 {ECO:0000313|EMBL:GCD19194.1};
OS   Cellulomonas algicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=2071633 {ECO:0000313|EMBL:GCD19194.1, ECO:0000313|Proteomes:UP000288246};
RN   [1] {ECO:0000313|EMBL:GCD19194.1, ECO:0000313|Proteomes:UP000288246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKZ-21 {ECO:0000313|EMBL:GCD19194.1,
RC   ECO:0000313|Proteomes:UP000288246};
RA   Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA   Otoguro M., Yanagida F., Hayakawa M.;
RT   "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL   Submitted (NOV-2018) 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}.
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:GCD19194.1}.
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DR   EMBL; BHYL01000054; GCD19194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401UX37; -.
DR   Proteomes; UP000288246; 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; 3.30.190.20; -; 1.
DR   Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR   Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 3.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   HAMAP; MF_00205; UvrA; 1.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
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; 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};
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};
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          608..936
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         739..765
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         27..34
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   952 AA;  104550 MW;  9EE38ECCA24E158B CRC64;
     MVQGAREHNL RNVDLDLPRD KLIVFTGLSG SGKSSLAFDT IFAEGQRRYV ESLSAYARQF
     LGQMDKPDVD FIEGLSPAVS IDQKSTNRNP RSTVGTITEV YDYLRLLFAR AGTQYCPECG
     ERVTAQTPQQ IVDRLLELPE GTRYQVLAPV VRGRKGEYAD LFKELQGKGF SRARVDGEVV
     QLTEPPTLEK KLKHDIEVVV DRLVSREGVQ RRLTDSVETA LGLAGGLLVV ELVDADADDP
     HRERRFSENR ACPNDHVLAL DEIEPRTFSF NAPYGACPEC TGIGSRLEVD PDLIVPDEDL
     SLDEGAVAPW AQISSEYFAR VLGALAQDMG FSTSVPWRAL PKRAKDAVLY GQNHEVKVRY
     KNRWGRERSY STGFEGVVTF LERRHSETES DWSKEKYEAF MREVPCPVCK GARLKPEVLA
     VRVGGKSIAD VCTLPIREAR TFLDGLELGE RERAIAAQVL KEIQARLGFL LDVGLDYLSL
     TRPAATLSGG EAQRIRLATQ IGSGLVGVLY VLDEPSIGLH QRDNRRLIDT LTRLRDLGNT
     LIVVEHDEDT IRTADWIVDI GPGAGEHGGR VVHSGDFTGL LKAKESVTGA YLSGRRSIPM
     PVERRKVDRE RQLTVVGARE HNLQGIDVSF PLGTLTAVTG VSGSGKSTLV NSILYTVLAN
     ELNGARQVAG RHKRVTGLEH LDKVVHVDQG PIGRTPRSNP ATYTGVWDHV RRLFAETTEA
     KVRGYTPGRF SFNVKGGRCE ACSGDGTLKI EMNFLPDVYV PCEVCHGARY NRETLEVHFK
     GKTVADVLAM PIEEAAEFFA AVPAISRHLR TLVDVGLGYV RLGQPAPTLS GGEAQRVKLA
     AELQRRSTGR TIYVLDEPTT GLHFEDIRKL LGVLQSLVDK GNSVIVIEHN LDVIKNADWI
     VDMGPEGGSG GGTVVAEGTP EHVAGVAASH TGRFLAEVLE AEVDQERERA TA
//
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