ID A0A1F1DWA2_9PORP Unreviewed; 862 AA.
AC A0A1F1DWA2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=HMPREF2890_05920 {ECO:0000313|EMBL:OFR34456.1};
OS Porphyromonas sp. HMSC065F10.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1739394 {ECO:0000313|EMBL:OFR34456.1, ECO:0000313|Proteomes:UP000177035};
RN [1] {ECO:0000313|EMBL:OFR34456.1, ECO:0000313|Proteomes:UP000177035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC065F10 {ECO:0000313|EMBL:OFR34456.1,
RC ECO:0000313|Proteomes:UP000177035};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:OFR34456.1}.
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DR EMBL; LTXH01000165; OFR34456.1; -; Genomic_DNA.
DR RefSeq; WP_070466532.1; NZ_KV793797.1.
DR AlphaFoldDB; A0A1F1DWA2; -.
DR STRING; 1739394.HMPREF2890_05920; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000177035; 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:UP000177035};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 15..469
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 817..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 862 AA; 96849 MW; 07E81F63E89C92B8 CRC64;
MNEEFKDSEN RIIKVDLEQE MKTSYIDYAM SVIVSRALPD VRDGFKPVHR RILFGMNDLG
NTPDKPYKKS ARIVGDVMGK YHPHGDSSIY MALVRMAQDW SMRNTLVDPH GNFGSVDGDG
PAAMRYTEAR LAPIAMEMLA DIKKETVDMT PNYDNSEYEP TVLPTRIPNL LVNGAAGIAV
GMATNMAPHN LTEVMNGVIA YIEKRGDVTT EDLMKHVKAP DFPTGGVIYG YKGVREAYET
GRGSIIIRGK AVIESSANHD QIIITEIPYG VVKKDLVKAI ADLATIKRIE GISNIQDESS
AKTGMRIVID IKRDANAGVV LNKLYKMTAL QSSFACNNIA LVDGRPRLLS LKELIGEFVK
HRHEVVTRRT RFDLRKAKER LHILEGRIIA ADNIDEVVHL IKASANQTAA MQALIERFSL
SEIQARSIVE MRLGQLTGLE LDKLHQEYDE VTEKVRYYER ILSDEDFLYS ILIDECREII
DKYGDDRRSE IVYATPDMNP EDFYPDDDMI ITISHYGYIK RTPLAEYRSQ NRGGTGAKGA
GTKDEDFVEF VYGASNHAHL LFFTDRGRCY WLRVFEIPEA ARNSKGRAIQ NILNIESDNR
ITAILRIKNL TSDQDFVDTH YLNFVTEQGM IRKARLRDFS RPRAKGIIAI RLKDETDRVV
SVMLTNGRHD VLLASREGRA IRFPESLLRP MGRSSAGVRG MRLQSPEDRV VGAISIKDPE
EESILVVSEN GYGKRSPLEE YRITNRGGKG IITLKATEKT GKLIAVHSVT DDHDIMIINK
SGVVIRVHVS DISILGRNTQ GIRLINLSKR DDEIADVCRV PADEDQAEQE DTSIGEREED
ADPTTLDEPE ETGDDTPESE ED
//
