ID F8KSQ1_HELBC Unreviewed; 804 AA.
AC F8KSQ1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 OrderedLocusNames=HBZC1_08440 {ECO:0000313|EMBL:CCB79830.1};
OS Helicobacter bizzozeronii (strain CIII-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1002804 {ECO:0000313|EMBL:CCB79830.1, ECO:0000313|Proteomes:UP000008387};
RN [1] {ECO:0000313|EMBL:CCB79830.1, ECO:0000313|Proteomes:UP000008387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIII-1 {ECO:0000313|EMBL:CCB79830.1,
RC ECO:0000313|Proteomes:UP000008387};
RX PubMed=21705603; DOI=10.1128/JB.05439-11;
RA Schott T., Rossi M., Hanninen M.L.;
RT "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an isolate
RT from human gastric mucosa.";
RL J. Bacteriol. 193:4565-4566(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR871757; CCB79830.1; -; Genomic_DNA.
DR RefSeq; WP_013890289.1; NC_015674.1.
DR AlphaFoldDB; F8KSQ1; -.
DR STRING; 1002804.HBZC1_08440; -.
DR KEGG; hbi:HBZC1_08440; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_7; -.
DR Proteomes; UP000008387; Chromosome.
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:UP000008387};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 6..458
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 519..525
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 117
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 804 AA; 89236 MW; 4BD6383290B86CA5 CRC64;
MEIKDVKIEE SLQESYLDYS MSVIVGRALP DARDGLKPVH RRILYAMHEL GLGSKVGYKK
SARIVGDVIG KYHPHGDSAV YEALVRMAQD FSMRLPLVDG QGNFGSIDGD NAAAMRYTEA
RMAAPSEELL RDIEKDTVDF NDNYDSTLKE PDILPSRLPN LLINGSSGIA VGMATSIPPH
RPSEIIDALV LVLDNPQIDL LSILEVIQGP DFPTGGIIYG KAGILEAYST GRGRVKLRAK
SRFEQIGQRE QIIIEEIPYQ TNKAKLVEQI SELARDKIIE GIAEVRDESD REGVRVVIEL
KKDAIAQIVL NHLYKSSALE STFSMILLAI YNKEPRIFNL LELLKLFLVH RKTIVIRRTI
FELEKARARV HILKGLLIAL QNSEAVIALI KSSADTLGAK EALAKAHHLS EEQSKAILDM
RLQRLTGLEQ EKIQQEHTQL QERIGYLQGI LENADKLNNL IKEELLEIKE KFDSPRLTQI
EEDYETLGVE DLIAHEDMVV TLSHRGYVKR MPLKVYEQQR RGGKGKISGN THEDDFIEFF
FSANTHDTIL FVTNMGQLYW LKVYRIPEMG RSAIGKALVN LIDLQPGERI KATLSTADFS
PDKSLVFFTK KGLIKRTNLS AFGRTRGGVR AIVLDEDDAF VTAQILNSGT QELFMASSKG
MCIRFGIEGV REIGRVARGV IGMRLRAGDE VIGGGVISSE QEKLLSVSSK GLGKQTLAGA
YRLQGRGGMG VIAMKITPKT GDLIGIVSVD ESQDLMILTK SGKMIRMPME SIRETGRNAS
GVKLVSVEGD VVVYANTCPK EESE
//
