ID A0A1N7LD72_9RHOB Unreviewed; 921 AA.
AC A0A1N7LD72;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=SAMN05421759_102601 {ECO:0000313|EMBL:SIS71774.1};
OS Roseivivax lentus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=633194 {ECO:0000313|EMBL:SIS71774.1, ECO:0000313|Proteomes:UP000186684};
RN [1] {ECO:0000313|EMBL:SIS71774.1, ECO:0000313|Proteomes:UP000186684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29430 {ECO:0000313|EMBL:SIS71774.1,
RC ECO:0000313|Proteomes:UP000186684};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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 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|ARBA:ARBA00008263}.
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DR EMBL; FTOQ01000002; SIS71774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7LD72; -.
DR STRING; 633194.SAMN05421759_102601; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000186684; 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};
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 COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 921 AA; 101386 MW; FEFD4AEEC196B6EE CRC64;
MTDTPEPPEN ADDMPPPPAP KTGPSISIEQ EMKSSYLDYA MSVIVSRAIP DLRDGLKPVH
RRILYAMHET GNTHDKSYRK SARPVGDVMG KYHPHGDSAI YDALVRMAQD FSMSLPLLDG
QGNFGSMDGD NPAAMRYTEV RMDKPAAYVL ADIDKDTVDF QDNYDGKDRE PTVLPARFPN
MLVNGAGGIA VGMATNIPPH NLGEVIDATL ALIDEPDLSS EALIEYIPGP DFPTGGIMLG
RSGARKAYLE GRGSVIVRSK TRIEELRKDR YAIVIDEIPY QVNKSAMIEK IAEAARDKKI
EGIAHVQDES DRNGVRVVVE LKRDATPDVV LNQLFRFTPM QTYFGCNMLA LNGGKPEQLT
LRRFLTSFID FREDVVARRT AYLLRKARER SHILCGLAVA VSNVDEVVAT IRASQDAAEA
REKLMTRRWP AGEIAPFIRL IDDPTHTMND DGTYNLSEAQ ARAILELRLQ RLTQLGVKEV
TDELEELAGK IKEYLEILGS RERIMGIISD ELREVKELFA VPRRTEIVDW SGDMEDEDLI
ERQDMVVTVT AGGYIKRTPL ADFRSQKRGG KGLSGGTLKD DDAVTTLFVA NTHTQLLVFT
TEGMVYKLKT WRLPLGGRTS KGKAIVNILP IPTGVSIAAI MPVDRDEEDW DDLQIVFATS
AGDVRRNALS DFTNVKRNGK IAMDLSEGVS LVNARIASED DDIMLVTDSG RAIRFRTTDV
RVFKGRKSTG VRGIKLSGDD HVVSMAVIRH SRYTPEERTA YLKMRRAMAG LSDEAEAGDE
EGVVADPNFS TELYAEMSAA ENLILTITRE GAGKLSSSHD YPIRGRGGMG VQAMDKAMRG
GPVVACFPVD LDDQIMLATS KGQSIRVPVE GISFRSRSAG GVRVFNTAKG EEVVSVAWIA
DQPEDEVGLI ADSDGDDPDE S
//