ID A0A345QN67_9RHOB Unreviewed; 916 AA.
AC A0A345QN67;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=C1J03_12410 {ECO:0000313|EMBL:AXI46754.1};
OS Sulfitobacter sp. SK012.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389005 {ECO:0000313|EMBL:AXI46754.1, ECO:0000313|Proteomes:UP000253903};
RN [1] {ECO:0000313|EMBL:AXI46754.1, ECO:0000313|Proteomes:UP000253903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK012 {ECO:0000313|EMBL:AXI46754.1,
RC ECO:0000313|Proteomes:UP000253903};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL Submitted (JAN-2018) 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}.
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DR EMBL; CP025804; AXI46754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345QN67; -.
DR KEGG; sulz:C1J03_12410; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000253903; 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:UP000253903};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 26..505
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 566..572
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 137
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 916 AA; 101462 MW; F79932A43A463231 CRC64;
MNDTPETPEN EDENRPERPV YDGPSVTIEE EMKTSYLDYA MSVIVSRAIP DLRDGLKPVH
RRILYAMHET NNTHDKPYRK SSRPVAEAMG KYHPHGDSAI YDALVRMAQS FSMSLVLLDG
QGNFGSMDGD KAAAYRYTEV RMKKAAQFLL EDIDKDTVDF QDNYDGKDRE PTVLPARFPN
MLVNGAGGIA VGMATNIPPH NLGEVIDATL ALIVEPDLTS EQLIDYIPGP DFPTGGLMLG
RTGARKAYLE GRGSVIVRAK TRVEEIRKDR YAIVIDEIPY QVNKSAMIEK IAEQVREKKI
EGIAHVQDES DRNGVRVVVE LKRDATAEVV MNQLFRFTPM QTYFGCNMLA LNGGRPEQLT
LRRFLTSFID FREDVVARRT AYLLRKARER SHILCGLAVA VTNIDEIVAT IRSSADAGEA
REKLMTRRWP AAEILPYIAL IDDPTHTAND DGTYNLSEAQ ARAILELRLQ RLTQIGVKEV
TDELEELAGK IKEYLEILGS RERIMGIISD ELQEVKDLFA VPRRTEIVDW SGDMEDEDLI
AREDMVVTVT SGGYIKRTPL VDFRSQRRGG KGVSGMQTKE EDVVTTLFVA NTHTQLLFFT
TDGMVYKLKT WRLPQGGRTS KGKAIVNILP IPVGVSIAAI MPVDRDESEW ADLQVVFSTS
AGTVRRNKLS DFTNVMRNGK IAMKFEDEHA GTTLINARIA SNDDDVMLTT NSGRAIRFPA
TDVRVFNSRA SVGVRGIRLS GDDAVVSMSI IRHFDATSEE RVAYLKMRRA VAGLADDTEV
GEDDEVVANA TISQERYAEM SASENLILTI SAKGSGKLSS SHDYPVRGRG GLGVTAMDKA
MRGGDIVASF PVELDDQIML ATSKGQSIRV PIEGISFRSR SAGGVKVFDT GRGEVVVSVA
WIADQGDEEE GEQPEE
//
