ID A0A1T5B2F9_9SPHI Unreviewed; 853 AA.
AC A0A1T5B2F9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=SAMN05660226_01286 {ECO:0000313|EMBL:SKB41365.1};
OS Parapedobacter luteus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=623280 {ECO:0000313|EMBL:SKB41365.1, ECO:0000313|Proteomes:UP000190541};
RN [1] {ECO:0000313|EMBL:SKB41365.1, ECO:0000313|Proteomes:UP000190541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22899 {ECO:0000313|EMBL:SKB41365.1,
RC ECO:0000313|Proteomes:UP000190541};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01897}.
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DR EMBL; FUYS01000002; SKB41365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5B2F9; -.
DR STRING; 623280.SAMN05660226_01286; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000190541; Unassembled WGS sequence.
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:UP000190541};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 21..474
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 820..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 853 AA; 95832 MW; F1192D84252BD01D CRC64;
MAEETENDNN LLPADDRIIP INIEDQMKSA YIDYSMSVIV SRALPDVRDG LKPVHRRVLY
GMLDLGVTSG KPYKKSARIV GDVLGKYHPH GDSSVYDTMV RMAQEWSLRY PLVDGQGNYG
SVDGDPPAAM RYTEARLKKI AEELLSDINK DTIDYQLNFD DSLEEPTVLP TRIPNLLVNG
ASGIAVGMAT NMAPHNLSEV VDGIVAYIDN RDIEIAELMQ YIKAPDFPTG AIIYGHAGVQ
EAFQTGRGRI VMRAKAEIET TKSGREQIIV TEIPYQVNKS DMIKRTADLV NEKKLEGISE
IRDESDRHGM RIVYDIKRDA NASIVLNNLY KYTALQTSFS VNNIALVHGR PMLLNLKDMI
YHFVEHRHEV VVRRTRFELA EAEKRAHILE GLLIALDHLD EVIQLIRSSA TPDDARVGLM
EKFGLSDIQA RAILDMTLRR LTGLERDKIK EEYAELMKTI EYLKSVLEDE GLRMKIIKDE
LLEIKDKYGD ERRSTIVHSA EDMRMEDFIE DEEVVITISH ESYVKRTPLS EYRRQSRGGK
GSLGTNTREE DFTEHIITAS AHNYMLFFTE AGRCFWLRAF EIPEGSRTSR GRAIQNIINI
PKEEKIKAYI KVKNLRDQEY LENNFIIMCT KRGTIKKTSL EAYSRPRANG INAINIAEGD
QLLEACLTDG GSEIVMALRS GRAIRFNEST VRPMGRTATG VRGVTLAGPD DEVVGMISVN
NSETTVLVVS EKGYGKRTDI EDYRVTNRGG KGVKTINVTE KTGKLVAIKD VTDNDDLMII
NKSGIVIRIA VSELRVMGRA TQGVRLISLK GDDEIASVAK VEHEEEELND ENQASSENTD
ENNSESTQSE SDD
//
