(data stored in SCRATCH zone)

SWISSPROT: C8VVA3_DESAS

ID   C8VVA3_DESAS            Unreviewed;       811 AA.
AC   C8VVA3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.3 {ECO:0000256|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN   OrderedLocusNames=Dtox_0007 {ECO:0000313|EMBL:ACV60972.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV60972.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV60972.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils
CC       closed circular double-stranded (ds) DNA in an ATP-dependent
CC       manner to modulate DNA topology and maintain chromosomes in an
CC       underwound state. Negative supercoiling favors strand separation,
CC       and DNA replication, transcription, recombination and repair, all
CC       of which involve strand separation. Also able to catalyze the
CC       interconversion of other topological isomers of dsDNA rings,
CC       including catenanes and knotted rings. Type II topoisomerases
CC       break and join 2 DNA strands simultaneously in an ATP-dependent
CC       manner. {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01897, ECO:0000256|SAAS:SAAS01173059};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       In the heterotetramer, GyrA contains the active site tyrosine that
CC       forms a transient covalent intermediate with DNA, while GyrB binds
CC       cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-
CC       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
CC       topoisomerases; in organisms with a single type II topoisomerase
CC       this enzyme also has to decatenate newly replicated chromosomes.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|SAAS:SAAS01062860}.
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DR   EMBL; CP001720; ACV60972.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0007; -.
DR   EnsemblBacteria; ACV60972; ACV60972; Dtox_0007.
DR   KEGG; dae:Dtox_0007; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076279; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   BioCyc; DACE485916:G1GFV-7-MONOMER; -.
DR   Proteomes; UP000002217; 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:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 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; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VVA3.
DR   SWISS-2DPAGE; C8VVA3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062880}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062879};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00972514, ECO:0000313|EMBL:ACV60972.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062871};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   DOMAIN        9    462       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   COILED      427    454       {ECO:0000256|SAM:Coils}.
FT   MOTIF       523    529       GyrA-box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01897}.
FT   ACT_SITE    120    120       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01897}.
SQ   SEQUENCE   811 AA;  90538 MW;  FFBF8B24BA06B5D5 CRC64;
     MSAGKVVPIN LKDEMKNSYM DYAMSVIVGR ALPDVRDGLK PVHRRIIYAM HGLGMTPDKA
     HKKCAHIVGE VLAKYHPHGD VAVYDALVRM AQSFSIRYTL VDGHGNFGSV DGDSAAAMRY
     TEARMTKIAT EMLTDIEKET VDFIPNYDES IEEPTVLPAR VPNLLINGSS GIAVGMATNI
     PPHNLAEVID GVIMLVDNPE ADSRTLMKAV KGPDFPTAGK IMGVQGIISA YTTGRGSIKI
     RAQAEIEEMS GGKNRIVVNE IPYQVNKARL IEKIAELVRD KKIEGISDLR DESDRKGMRI
     VIELKRDVYP QLVLNQLYKH TKMQDSFGVI MLALVDGRPN VLNLRDMLYY YLEHQKDIII
     RRTTFDLKKA EARAHIVEGL RIALANLDEV INTIRSSQTV EIAKQGLVEK FLLTEIQAQA
     ILEMRLQRLT GLEIEKLEQE YRDLMEKIAY LEAILSDEGK ILAIIKDELL EIRKKYADKR
     RTVISDEDTA FDVEDLIAEE DMVITITRNG YIKRLPLDTY RSQKRGGRGI SAMGVKEKDF
     LKHLFITSTH HYILFFTNKG KVYRLKVHEI PEAGRQSKGT AIINLLFVGT EEKVTTVIPV
     KEFNKDEFLF MCTKNGIVKK TSLNEFDTSR RDGIIALTLD DHDDLVDVRL TNGQEEIIIG
     TQKGLAIRFS EDDVRKLGRI AKGVRGIGLI EGDFVVGMDT VRNEGDLLVV TKNGFGKKTP
     ISEYRLQTRG GKGIINVKIS DRNGPVVSLL VVKPDEEIMM LSSEGIIIRM KVNEISTTGR
     ATQGVTLMKL SSGDSVATIA KVNAEVDADV E
//

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