ID A0A1K1PHZ0_9FLAO Unreviewed; 840 AA.
AC A0A1K1PHZ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=SAMN02927921_01740 {ECO:0000313|EMBL:SFW46278.1};
OS Sinomicrobium oceani.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sinomicrobium.
OX NCBI_TaxID=1150368 {ECO:0000313|EMBL:SFW46278.1, ECO:0000313|Proteomes:UP000182248};
RN [1] {ECO:0000313|EMBL:SFW46278.1, ECO:0000313|Proteomes:UP000182248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12145 {ECO:0000313|EMBL:SFW46278.1,
RC ECO:0000313|Proteomes:UP000182248};
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 type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
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DR EMBL; FPJE01000008; SFW46278.1; -; Genomic_DNA.
DR RefSeq; WP_072316977.1; NZ_FPJE01000008.1.
DR AlphaFoldDB; A0A1K1PHZ0; -.
DR STRING; 1150368.SAMN02927921_01740; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000182248; 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; 7.
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}; Reference proteome {ECO:0000313|Proteomes:UP000182248};
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 COILED 434..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 840 AA; 94468 MW; 9A11A72226EBB1B8 CRC64;
MAEGEKLIPI NIEDEMKSAY IDYSMSVIVS RALPDVRDGL KPVHRRVLFG MYELGVLSNR
PYKKSARIVG EVLGKYHPHG DSSVYDTMVR MAQEWSLRYM LVDGQGNFGS VDGDPPAAMR
YTEARMRKIS EDMLADIDKE TVDHSLNFDD TLKEPTVLPT RVPNLLVNGA SGIAVGMATN
MPPHNLAEVV DGTIAYIDNH DIEIDELIQH IKAPDFPTGG IIYGYDGVRE AFKTGKGRVV
IRAKAVIEEV QGRECIIVTE IPYQVNKAEM IKKTADLVNE KKLEGISNIR DESDRNGMRI
VYVLKRDAIP NIVLNTLYKY TALQSSFSVN NIALVKGRPQ LLNLKEMIHH FVEHRHEVVV
RRTEYELKKA EERAHILEGL IIASDNIDEV IAIIRGSSNA EEARGKLMER FSLSEVQARA
IVEMRLRQLT GLEQDKLRAE YEEIKQLIEE LKDILARKER RMEIIKEELQ EVRDKYGDPR
RSTIEYAGGD LSIEDMIPDE QVVITISHAG YIKRTSLSEY KTQNRGGVGQ KASNTRNEDF
LEHLFVGTNH QYMIFFTQKG KCFWLRVYEI PEGTRTSKGR AIQNLINIEQ DDKVKAFICT
KDLKDEAYIN NHYVIMATKK GIVKKTSLEQ YSRPRQNGIN AITIREDDEL LEAKLTTGTS
QVMLAVQSGK AVRFEEEKTR PMGRNASGVR GITLADDSDE VVGMITIDNP QEESVLVVSE
NGYGKRTFID DPEDGSPIYR ITNRGGKGVK TISITEKTGK LVAIKSVSDT DDLMIINKSG
IAIRLKVSDL RVMGRATQGV RLISIKGKDS IAAVAKVMRE EEAEDLELDG TDTDITEADV
//