ID A0A430FHG8_9BIFI Unreviewed; 898 AA.
AC A0A430FHG8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D2E25_1549 {ECO:0000313|EMBL:RSX52138.1};
OS Bifidobacterium goeldii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2306975 {ECO:0000313|EMBL:RSX52138.1, ECO:0000313|Proteomes:UP000287533};
RN [1] {ECO:0000313|EMBL:RSX52138.1, ECO:0000313|Proteomes:UP000287533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2034B {ECO:0000313|EMBL:RSX52138.1,
RC ECO:0000313|Proteomes:UP000287533};
RA Lugli G.A., Duranti S., Milani C.;
RT "Characterization of the phylogenetic diversity of five novel species
RT belonging to the genus Bifidobacterium.";
RL Submitted (SEP-2018) 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}.
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:RSX52138.1}.
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DR EMBL; QXGL01000005; RSX52138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430FHG8; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000287533; 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}; Reference proteome {ECO:0000313|Proteomes:UP000287533};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 44..501
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 562..568
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 843..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 898 AA; 100096 MW; 93F4246463B4EAC1 CRC64;
MADENGTGND LPEQNDERAE RSMEPTSPQA NEQLVLDEHR VAHTDIQKEM RQSYLDYAIS
VIVERALPDV RDGMKPVHRR IVYAMYDGGY RPDRGYSKCA RPVADVMGNY HPHGDVAIYD
TLVRMAQPWS MRYTLVDGQG NFGSAGDDPP AAMRYTECRM MPLAMEMVRD IDKDTVDFVP
NYDGRTQEPT VLPARFPNLL ANGSSGIAVG MATNIPPHNM RELATAVHWT LDHPEASREE
LLDALIGIIK GPDFPTGATI LGHKGIEQAY RTGRGLITMR AVVNTEEIKG RMCLVVTELP
YQVNPDRLAA SIREGVRDGK IQGIADMRDE TSGRTGQRLV LVLKRDAVPK VVLNNLYKHS
QLQQTFGANM LALVDGVPRT LSLDAFIRHW VSHQLEVIER RTRYLKREAE ERDHILQGLL
KAMDAIDEVI RLIRSSQGRE DARPKLMEFL DIDQVQADAI LSMQLVRLAN MERQKIVDEH
EELMRKIADY NDILAKPERQ RKIVGDELDE IVAKYGDDRR TKILPYSGEM NVEDLIAEEN
VVVTVTHSGF IKRTKADEYR AQHRGGKGIK GAKLREDDVV DHFFLTSTHN WLLFFTNKGR
VYRIKAYELP EGSRDSKGQH VANLLQFGPD ETIQTVLSIP NYEVAKYLVL ATRSGKVKKT
ALAEYDSPRQ GGLIAVRLMT DENGENADEL IGAALCNAED DIILVSRQGM SLKFAADDEQ
LRPMGRQTAG VQGMKFRDDD ELLAMDVVPA DTDKDLLVVT NEGFAKRTAI SEYRLQGRNG
FGVKALQLAE GRGSLVGAVV VSEDDQVMAI MKSGKVIRSD VAEVKRTGRT TQGVTLAKPD
KNDEIISIAR NEEKDDDDET AAQASAAESA ESAESVEPTS DAASEASDEN VNKTDDEE
//
