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Database: UniProt
Entry: A0A1N7LD72_9RHOB
LinkDB: A0A1N7LD72_9RHOB
Original site: A0A1N7LD72_9RHOB 
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
//
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