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Database: UniProt
Entry: A0A1K1LR28_9FLAO
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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
//
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