ID K2PIZ3_9LACT Unreviewed; 824 AA.
AC K2PIZ3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=C426_1214 {ECO:0000313|EMBL:EKF51400.1};
OS Lactococcus garvieae DCC43.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1231377 {ECO:0000313|EMBL:EKF51400.1, ECO:0000313|Proteomes:UP000006787};
RN [1] {ECO:0000313|EMBL:EKF51400.1, ECO:0000313|Proteomes:UP000006787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCC43 {ECO:0000313|EMBL:EKF51400.1,
RC ECO:0000313|Proteomes:UP000006787};
RX PubMed=23209230; DOI=10.1128/JB.01864-12;
RA Gabrielsen C., Brede D.A., Hernandez P.E., Nes I.F., Diep D.B.;
RT "Genome Sequence of the Bacteriocin-Producing Strain Lactococcus garvieae
RT DCC43.";
RL J. Bacteriol. 194:6976-6977(2012).
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:EKF51400.1}.
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DR EMBL; AMQS01000014; EKF51400.1; -; Genomic_DNA.
DR RefSeq; WP_003135731.1; NZ_AMQS01000014.1.
DR AlphaFoldDB; K2PIZ3; -.
DR PATRIC; fig|1231377.3.peg.1215; -.
DR eggNOG; COG0188; Bacteria.
DR Proteomes; UP000006787; 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 9..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 524..530
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 824 AA; 92264 MW; A067CF0F409163BA CRC64;
MEDKNIINVN LAEEMKTSFR DYAMSVIVAR ALPDVRDGLK PVHRRILYGM NELGTTPDKP
HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRHML VDGHGNFGSM DGDGAAAQRY
TEARMSKIAL EMLRDINKNT VDFVDNYDGT EREPEVLPAR FPNLLVNGTT GIAVGMATNI
PPHNLGETID AVDLLMENPE VTTRDLMEVL PGPDFPTGAL VMGKSGIRRA YETGKGSITL
RAKTEIEELP GGKERIVVTE FPYMVNKSKV HEHIVRLAQE KRIEGVTACR DESSREGVRL
VVEVRRDASA HVILNNLFKL TQLQTSFGFN MLAIENGTPK ILSLKQILTE YIAHQIEVVE
RRTRFDKARA EARAHILEGL RIALDNIDRM ITIIRESATD AIAQKAMMDE FQLSDKQSQA
ILDMRLRRLT GLERDKIENE YQELIALIAD LADILAKPER VKAIIREELG EIKRKFADAR
RTELLVGEVL NLEDEDLIEE EDVLITLSNK GYIKRLSNDE FRSQKRGGRG VQGMNMTDDD
FVQHLVSSST HDNLLFFTNQ GRVYRMKGYE IPEYGRTAKG LPIVNLLKLD EGEKIQTVIN
VVKSDEERYL FFTTRNGLVK RTNTKQFANI RTNGLKALNL RDGDELINVL LTSGDENIII
GTHNGFSVRF RESVVRDMGR SATGVKGVSL REGDFVVGTA TVYDEQEVLV ISEKGLGKRT
IASEYPTKGR GGKGIKVMNV TERTGKLAGL TAINGNEDIM VITDTGVVIR TSVENISQTG
RAAQGVKIMR LDDEAQIVTF ALVEPEAEDD EELNEAETVS NTEE
//
