ID   C5BUP9_BEUC1            Unreviewed;       885 AA.
AC   C5BUP9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN   OrderedLocusNames=Bcav_0007 {ECO:0000313|EMBL:ACQ78273.1};
OS   Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC   Beutenbergia.
OX   NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ78273.1, ECO:0000313|Proteomes:UP000007962};
RN   [1] {ECO:0000313|EMBL:ACQ78273.1, ECO:0000313|Proteomes:UP000007962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC   {ECO:0000313|Proteomes:UP000007962};
RX   PubMed=21304633; DOI=10.4056/sigs.1162;
RA   Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA   Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT   0122).";
RL   Stand. Genomic Sci. 1:21-28(2009).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC       circular double-stranded (ds) DNA in an ATP-dependent manner to
CC       modulate DNA topology and maintain chromosomes in an underwound state.
CC       Negative supercoiling favors strand separation, and DNA replication,
CC       transcription, recombination and repair, all of which involve strand
CC       separation. Also able to catalyze the interconversion of other
CC       topological isomers of dsDNA rings, including catenanes and knotted
CC       rings. Type II topoisomerases break and join 2 DNA strands
CC       simultaneously in an ATP-dependent manner. {ECO:0000256|HAMAP-
CC       Rule:MF_01897}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC         ECO:0000256|HAMAP-Rule:MF_01897};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC       the heterotetramer, GyrA contains the active site tyrosine that forms a
CC       transient covalent intermediate with DNA, while GyrB binds cofactors
CC       and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils. Not all organisms have 2 type II topoisomerases;
CC       in organisms with a single type II topoisomerase this enzyme also has
CC       to decatenate newly replicated chromosomes. {ECO:0000256|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC       Rule:MF_01897}.
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DR   EMBL; CP001618; ACQ78273.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5BUP9; -.
DR   STRING; 471853.Bcav_0007; -.
DR   KEGG; bcv:Bcav_0007; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_11; -.
DR   Proteomes; UP000007962; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   HAMAP; MF_01897; GyrA; 1.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   NCBIfam; TIGR01063; gyrA; 1.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01897}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01897};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000007962};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_01897}.
FT   DOMAIN          35..492
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          844..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           553..559
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        146
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   885 AA;  97172 MW;  6CF4CDD25D407D2E CRC64;
     MTQPPETPDE RDAETTDAVV SAAGASALRD RVEQVDLQLE MQRSYLDYAM SVIVGRALPE
     VRDGLKPVHR RVLYAMFDGG YRPDSAFSKC ARVVGDVMGN YHPHGDTAIY DALVRLVQPW
     SMRYPLVAGQ GNFGSPGDDS AAAPRYTECK MAPLAMEMVR DIDKDTVDFG DNYDGRTQEP
     LILPARFPNL LVNGSAGIAV GMATNIPPHN LREVAEGVEW FLEHPDATNE ELLGALLLRI
     KGPDFPTGAQ ILGHRGIEDA YRTGRGSITM RAVVEVEEIQ GRQCLVVTEL PYQVNPDRLA
     AKIGEMVREG RISGIADLRD ETSGRAGQRL VIVLKRDAVA KVVLNNLYKH TQLQDTFGAN
     MLALVDGVPR TLSLDAFVRH WTMHQIDVIV RRTRYLLAED ERRIHILRGL LKALNALDEV
     IALIRRSPSS DEARTGLMEL LEIDEVQATA ILDMQLRRLA ALEQQRIMDE HAAIEARILD
     YQDILASEER QRSIVRSELG AIVERYGDER RTTILPFDGE MSVEDLIPEE DVVVTITRGG
     YAKRTRTDNY RAQRRGGKGV RGAQLREDDV VDHFFVTTTH HWLLFFTNLG RVYRAKGYEL
     PEGGRDAKGQ HVANLLAFQP GEKIAQVLAL RDYDQADYLV LATKRGLVKK TRLAEYDSSR
     TGGVIAINLR TDDGGAVDEV VSARIVGAED DLLLVSRKGQ SIRFTATDEA LRPMARATSG
     VTGMKFRADD ELLAMDVVET DADLFVVTEG GFAKRTALGE YRVQGRGGLG IKVANLVEAR
     GDLVGALVVD SDDEVLVIME RGKIVRSAVD EVTRTGRNTQ GVTFAKPDAG DRIIAIALGE
     ERAVADAGEE PVEESAEGAP TTDPAEGDGV PSSPEAAPEA EEGQA
//