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Database: UniProt/TrEMBL
Entry: Q15T02_PSEA6
LinkDB: Q15T02_PSEA6
Original site: Q15T02_PSEA6 
ID   Q15T02_PSEA6            Unreviewed;       897 AA.
AC   Q15T02;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   01-MAY-2013, entry version 52.
DE   RecName: Full=DNA gyrase subunit A;
DE            EC=5.99.1.3;
GN   Name=gyrA; OrderedLocusNames=Patl_2470;
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC       stranded DNA in an ATP-dependent manner and also catalyzes the
CC       interconversion of other topological isomers of double-stranded
CC       DNA rings, including catenanes and knotted rings (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA.
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       Within the heterotetramer, GyrA contains the active site tyrosine
CC       that forms a covalent intermediate with the DNA, while GyrB
CC       contributes the cofactor binding sites and catalyzes ATP
CC       hydrolysis (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
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DR   EMBL; CP000388; ABG40986.1; -; Genomic_DNA.
DR   RefSeq; YP_662040.1; NC_008228.1.
DR   ProteinModelPortal; Q15T02; -.
DR   SMR; Q15T02; 30-521, 535-860.
DR   STRING; 342610.Patl_2470; -.
DR   EnsemblBacteria; ABG40986; ABG40986; Patl_2470.
DR   GeneID; 4174224; -.
DR   KEGG; pat:Patl_2470; -.
DR   PATRIC; 23050128; VBIPseAtl25434_2642.
DR   eggNOG; COG0188; -.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; IAQEDVV; -.
DR   BioCyc; PATL342610:GHGT-2554-MONOMER; -.
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:HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_01897; GyrA; 1; -.
DR   InterPro; IPR024946; Arg_repress_C-like.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_pinwhl.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
DR   InterPro; IPR013760; Topo_IIA_like_dom.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   TIGRFAMs; TIGR01063; gyrA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
FT   ACT_SITE    122    122       O-(5'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity).
SQ   SEQUENCE   897 AA;  99934 MW;  F4F51E3E5DB21B2A CRC64;
     MTDHAQEILP INIEEELKNS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMNELKNDFN
     KPYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SVDGDSAAAM
     RYTEIRMAKI SHELLADLEK ETVDFVPNYD GTEFIPDVLP TKVPNLLING SSGIAVGMAT
     NIPPHNLTEV VNGCIALIDK PELSIEELME YIPGPDFPTA AFISGRKGIE EAYRTGRGKI
     YMRARAEIER EDNGKETIVV HEIPYQVNKA RLIEKIAELV KEKKIEGISA LRDESDKDGM
     RIVVEVKRNE SGEVLLNHLY SQTQMQTVFG INMVALDKTQ PKVFNLLEIL QAFVLHRREV
     VTRRTVFELK KARERAHILE GLAIALANID PIIALIKASK SPSDAKISLT AQGWALGDVS
     DMLERAGNDA ARPDWLEPEF GIRDGLYYLT EQQAQAILDL RLNKLTGLEH EKILSEYKEL
     LDLIAELLHI LGSPERLMEV IREELEKIRD EFGDERRTEI TAASHDIDIE DLIEREEVVV
     TLSREGYVKY QKLNDYESQR RGGKGKSATK MKEEDFIEKL LVANTHDHIL CFSTRGRLYW
     LKVYQLPLAS RNARGRPIVN ILPLEANERI TAILPIQEFE EGKYVLMATA NGTVKKTALV
     QYSRPRANGI IAVNLNDGDE LIGVDITDGS SDIMLFSDAG KVVRFNEKAR DSETGAVKID
     PETGEEILAL RPMGRTATGV RGIRLQDGQK VVSLIVPQGD GAILTATENG FGKRTPVEDY
     PAKSRATQGV VSIKVSERNG KVVGAVQVND SDEIMLISDQ GTLVRTRVGE VSTVGRNTQG
     VRLIRTGEDE HVVGLQRIDE VEELEEELEA LAEGDETVEA AASDVDNTTD EDPQNEE
//
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