ID   GYRA_FIBSS              Reviewed;         903 AA.
AC   P35810; C9RKP7; D9S813;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897};
GN   OrderedLocusNames=Fisuc_0363, FSU_0778;
OS   Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC   Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae; Fibrobacter.
OX   NCBI_TaxID=59374;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19169 / S85;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Weimer P.J.,
RA   Stevenson D.M., Boyum J., Brumm P.I., Mead D.;
RT   "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19169 / S85;
RA   Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA   Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT   "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 709-903.
RX   PubMed=8244936; DOI=10.1128/jb.175.23.7666-7672.1993;
RA   Paradis F.W., Zhu H., Krell P.J., Phillips J.P., Forsberg C.W.;
RT   "The xynC gene from Fibrobacter succinogenes S85 codes for a xylanase with
RT   two similar catalytic domains.";
RL   J. Bacteriol. 175:7666-7672(1993).
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:0000255|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:0000255|HAMAP-
CC         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:0000255|HAMAP-Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_01897}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADL25539.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001792; ACX73975.1; -; Genomic_DNA.
DR   EMBL; CP002158; ADL25539.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U01037; AAA21849.1; -; Genomic_DNA.
DR   PIR; A53295; A53295.
DR   RefSeq; WP_012820205.1; NC_017448.1.
DR   AlphaFoldDB; P35810; -.
DR   SMR; P35810; -.
DR   STRING; 59374.Fisuc_0363; -.
DR   PRIDE; P35810; -.
DR   EnsemblBacteria; ADL25539; ADL25539; FSU_0778.
DR   KEGG; fsc:FSU_0778; -.
DR   KEGG; fsu:Fisuc_0363; -.
DR   PATRIC; fig|59374.8.peg.753; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_0; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   Proteomes; UP000000517; 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; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 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   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 2.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
FT   CHAIN           1..903
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145234"
FT   REGION          881..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           526..532
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        124
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   903 AA;  99633 MW;  68F9820762B8ED8D CRC64;
     MSEEMVPGSQ FKSLVEQDMQ DCYLRYSMSV IVARALPDAR DGFKPVHRRV MYSMHKLGVV
     PNKGTVKSAR IVGDVIGKYH PHGDVAVYDT LARMAQDFSL RYPLVFGQGN FGSIDGDSPA
     AMRYTEAKMN NLGALMLEDL EKETVDMGPN YDESLEEPLV LPSALPNMIV NGTSGIAVGM
     ATNMAPHNLR EVGAAIHALA ENPDLTGEDL MEYVKGPDFP TGAIVCGRSG IREAYLTGHG
     RVRVRARTEI ETDAKGKPRI IVTEIPYMVN KAELCKKIAD LVRDKRIDGI TDIRDESSRD
     IRIVIELRRD AVGEVVLNNL FKYTQLQTTF SIYNLALVNN LPKLLTLKDL LQVYIDHRLD
     VITRATQFDL KKAAARLHII EGLRIATQNI DEVVKIIRQS KTTEIAKQSL QDRFSLDEIQ
     SQAIVDMRLA QLVGLNIEKL EAEYNELIAT VADLKDILEK RERRVAIMLQ KLDAVVDKYG
     DERRTTIGEA IDDSDDEDLI AEEEQVITLS KEGYIRRLPI DTFKAQNRGG KGIIGAGLKD
     EDNVEQIFTA STHSYLLVFT NKGRVYWTKV YRLPEGARNG KGRPIVNFVA LTEGEKVQAI
     VPVRKFGGYF CLVFATKKGI INKMDLTLFS RPRKAGVNAI SLDEDDELVK VQLVGMSAEE
     YEASKNASDD DSAEAVENAA EAQAAEAAIA EESESGDAED FANRPIPKDL LMIATKNGQA
     VTFPISCFRA MGRGTHGVKG ITLAEGDEVI SLLWLKAGNK ILTITEKGYG KRSEPGSYRV
     TRRGSKGVRN LNVTDKIGAA VFVESVADDY DLIITSKDGQ VIRIKAADIR LTGRNAQGVK
     AITLRDGDVV KDATALPSVE DIEQDSADAK ETFDKVKGVE VDDDSVVKDD AEKQEIGPTE
     TEE