ID A0A2T7G321_9RHOB Unreviewed; 923 AA.
AC A0A2T7G321;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=DC366_17125 {ECO:0000313|EMBL:PVA08821.1};
OS Pelagivirga sediminicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pelagivirga.
OX NCBI_TaxID=2170575 {ECO:0000313|EMBL:PVA08821.1, ECO:0000313|Proteomes:UP000244446};
RN [1] {ECO:0000313|EMBL:PVA08821.1, ECO:0000313|Proteomes:UP000244446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH-SD19 {ECO:0000313|EMBL:PVA08821.1,
RC ECO:0000313|Proteomes:UP000244446};
RA Ji X.;
RT "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT Bohai Sea.";
RL Submitted (APR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVA08821.1}.
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DR EMBL; QCYH01000016; PVA08821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7G321; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000244446; 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:UP000244446};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 16..495
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 897..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 556..562
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 127
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 923 AA; 101247 MW; 044BDFD1245EA207 CRC64;
MDEMTPERPA YDGPTVSIAD EMKTSYLDYA MSVIVSRAIP DLRDGLKPVH RRILYAMHDA
GNTHDKPYRK SARAVGDVMG KYHPHGDSAI YDALVRMAQD FSMSLPLLDG QGNFGSMDGD
NAAAMRYTEV RMDKPAAYLL ADIDKETVDF QDNYDGKDRE PTVLPARFPN MLVNGAGGIA
VGMATNIPPH NLGEVVDATL ALIENPDLTS EDLIEYIPGP DFPTGGMMLG RSGARKAYLE
GRGSVIIRAK TRTEEIRKDR WAIIIDEIPY QVNKATMIER IAEAAREKRI EGIAHVQDES
DRDGVRVVIE LKRDATAEVV LNQLFRFTPM QTYFGCNMLA LNGGRPEQLT LRRFLTSFID
FREDVVARRT AHLLRKARER SHILCGLAVA VSNVDEVVAT IRASADAADA RQKLMERRWP
AGDILEYIAL IDDPTHTAND DGTYNLSEIQ ARAILELRLQ RLTQLGVKEV TDELQDLAGK
IKEYLAILAS RERIMEIIAN ELAEVRELFA VPRRTQIVDW SGDMDDEDLI EREDMVVTVT
SGGYIKRTAL ADFRSQKRGG KGVGGMATKD EDVVTTLFVA NTHTQLLFFT TDGMVYKLKT
WRLPQGGRTS KGKAIVNILP IPTGVSIAAI MPVDRDEAEW DDLQVVFATS AGTVRRNKLS
DFTNVRANGK IAMRFEEENA GITLINARIA SNEDDVMLVT SSGRAIRFPA TDVRVFNSRA
SLGVRGIRLT GDDSVVSMSI IPHFDATSDE RAAYLKMRRA QAGLTDEELE AADDEGDANA
DITQERFAAM SDAETLILTI TAQGTGKLSS SHDYPVRGRG GMGVAAMDRA MRGGPLVASF
PVTLEDQIML ATSKGQSIRV PVEGISFRSR SAGGVKVFDT GRNETVVSVA WIAEQSDDED
AIDGDAPVDT TGVQPGGTSS EGA
//
