ID A0A2J9E1H7_9GAMM Unreviewed; 941 AA.
AC A0A2J9E1H7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A6J60_012680 {ECO:0000313|EMBL:PNK61635.1};
OS Psychrobacter sp. FDAARGOS_221.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK61635.1, ECO:0000313|Proteomes:UP000217719};
RN [1] {ECO:0000313|Proteomes:UP000217719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_221 {ECO:0000313|Proteomes:UP000217719};
RA Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L.,
RA Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K.,
RA Aluvathingal J., Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2017) 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:PNK61635.1}.
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DR EMBL; NWFK02000001; PNK61635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J9E1H7; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000217719; 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 8..515
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 895..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 576..582
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 921..941
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 941 AA; 103576 MW; DE23E2A153F4C154 CRC64;
MSDSVSPIAI IDEMKQSYLD YAMSVIVSRA LPDVRDGLKP VHRRIMYAMH QLSNDYNKPY
KKSARVVGDV IGKYHPHGDT AVYDAIVRMA QDFSLRYPMV DGQGNFGSID DDPAAAMRYT
EVRMTKLTHK MLADLDKDTV DWEDNYDGSE RMPSVLPARI PNLLVNGATG IAVGMATNMA
PHNLTEVLNA CLAYADNPNI SSEELTNYIS GPDFPTGGII YGRAGIVDAY RTGKGRLHIR
GRYHIEPMSE TGANRERERI VFTEIPYQAN KAKLIERIAE LVRDKKIEGI SEIRDESDKD
GMRIAIDLRR GEVAEVIVNN LFLQTPLESS FSINMVALDN GQPKLMTLRQ LIAAFVRHRQ
EVVTRRTIYE LNKAKARGHL LEGLTVALAN IDDIIATIKE SANRGEAREK LLAQVWDSGT
VVAMLQAAGR GTLAAGDLRS VRPEFIEGED LKNPFGLIDD GNNYRLSLEQ VNAILEMQLH
RLTGLEQDKL TEEYQDILRQ IAELESILAD FDKLMMVIKN EMQEILDEFG DERRTDIVDS
RSDFSREDLI PEQTVVLTVS RTGYAKTQPI GDYVAQNRGG RGKSAAAMKE DDVIDHLVVT
STHATVLCFT DNGRVFSLRG FEVPIASRGA RGRPLVNIIG LDPDEIVTTI LPIPKAVEEA
PHDADEAAAI ADADVVDDDA EENDNTVTGP FVFFATANGT VKRVKLSQFA NIRSNGLIAI
GLEEDDKLVS ARITNGEQQV MLFASSGKAI RFDENDARVM GRTAKGVRGM RIAKDESIKS
LVVIEDDVKE ILIACENGYG KRTPAEEFNA QNRGGGGVIA IKTSERNGAL VRATKVHPED
DIILISNKGT LVRTPVAQVA TSGRNTQGVT LIRLANDEVL VGMARVEEST EEEELLEGML
DSTDAPSDAD EANKLADDVE TDSDTDIDDT DADNINDASD D
//
