ID A0A1K1LR28_9FLAO Unreviewed; 857 AA.
AC A0A1K1LR28;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=SAMN05660313_00008 {ECO:0000313|EMBL:SFW13319.1};
OS Cellulophaga fucicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=76595 {ECO:0000313|EMBL:SFW13319.1, ECO:0000313|Proteomes:UP000183257};
RN [1] {ECO:0000313|EMBL:SFW13319.1, ECO:0000313|Proteomes:UP000183257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24786 {ECO:0000313|EMBL:SFW13319.1,
RC ECO:0000313|Proteomes:UP000183257};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FPIY01000001; SFW13319.1; -; Genomic_DNA.
DR RefSeq; WP_072301723.1; NZ_FPIY01000001.1.
DR AlphaFoldDB; A0A1K1LR28; -.
DR STRING; 76595.SAMN05660313_00008; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000183257; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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 10..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 826..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 441..475
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 523..529
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 857 AA; 95743 MW; 949B312E73DD9F40 CRC64;
MAEGEKIIPI NIEDEMKSAY IDYSMSVIVS RALPDVRDGL KPVHRRVLYG MHELGVRSNS
AHKKSARIVG EVLGKYHPHG DTSVYDSMVR MAQEWSLRYM LVDGQGNFGS IDGDSPAAMR
YTEARMRKIA DDMLADIEKD TVDHQLNFDD SLKEPTVLPA RIPNLLVNGA SGIAVGMATN
MPPHNLTEVV DGTIAYIDNN DIEIDELITH IKAPDFPTGG IIYGYDGVRE AFKTGRGRVM
MRAKATFEEV QGRECIVVTE IPYQVNKADM IKKTADLVND KKIEGISTIR DESDRNGMRI
VYILKRDAIP NIVLNTLYKY TALQTSFSVN NIALVKGRPQ LLNVKEMIHY FVEHRHEVVV
RRTEFELKKA EDRAHILEGL IIASDNIDEV IAIIRGSSNA DEARENLIER FKLSEIQAKA
IVEMRLRQLT GLEQDKLRAE YDEIVKTIAD LKDILANQER RMQIIKDELL EVKEKYGDER
RSEINFAGGD LSIEDMIPDE QVVITISHAG YIKRTPLTEY KTQNRGGVGQ KASSTRTEDF
LEHLFVGTNH QYMLFFTQKG KCFWMRVYEI PEGSKTSKGR AIQNLINIEQ DDAVKAFICT
QDLKDEEYVN SHYVIMATKK GTVKKTSLEQ YSRPRLNGIN AIGIKDDDEL LEAKLTTGTS
QIFLGLKSGK AIRFEESKTR PMGRNASGVR GITLADDNDE VVGMVSVHNF DDDILVVSEK
GYGKRSSLED YRITNRGGKG VKTISVTDKT GGLVAIKNVT DSDDLMIINK SGIAIRMGVE
DLRVMGRATQ GVRLINIKGK DSIAAVAKVM KDEEAVIEDE LADGEEAIEG EALDITEGEG
TSEDGTALDN DTTESEE
//