ID A0A1N7FLH5_9GAMM Unreviewed; 892 AA.
AC A0A1N7FLH5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=SAMN02745664_11414 {ECO:0000313|EMBL:SIS01124.1};
OS Moraxella cuniculi DSM 21768.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1122245 {ECO:0000313|EMBL:SIS01124.1, ECO:0000313|Proteomes:UP000187495};
RN [1] {ECO:0000313|Proteomes:UP000187495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21768 {ECO:0000313|Proteomes:UP000187495};
RA Varghese N., Submissions S.;
RL Submitted (JAN-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}.
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DR EMBL; FTNU01000014; SIS01124.1; -; Genomic_DNA.
DR RefSeq; WP_076555744.1; NZ_FTNU01000014.1.
DR AlphaFoldDB; A0A1N7FLH5; -.
DR STRING; 34061.B0189_06320; -.
DR Proteomes; UP000187495; 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:UP000187495};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 8..507
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 568..574
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 892 AA; 98027 MW; 0AF76054597D52B3 CRC64;
MSDSVSPIGI VDELKRSYLD YAMSVIVSRA LPDVRDGLKP VHRRILYAMH ELGNDYNKKY
LKSARVVGDV IGKYHPHGDT AVYDAIVRMA QDFSLRYMLV NGQGNFGSMD GDPPAAMRYT
EMKMQKLTHK MLADLDKDTV DWEDNYDGSM KMPSVLPARI PNLLVNGAAG IAVGMATNMA
PHNLTEVLNA CLAYADNPNI STDELITHIS GPDFPTGGII YGRSGIVDAY RTGKGRLHIR
GRYHIEPMGE SGANKDRERI VFTEIPYQVN KANLIKHIAD LVNAKKIEGI TEIRDESDKE
GVRVAIDLRR GENAEVMVNN LFSQTPLETS FSINMVALDN GQPKLMTLKD LVAAFIRHRQ
EVVTRRTIFE LNKALVRGHL LEGLAIALAN IDEVLELIKN SANRSQARDN LLARTWQSAG
VVAMLEAAGA DSIRPEIIDG EDLNAPYGLI DGKTRYRLSP DQVNAILDMQ LHRLTGLEQD
KLTGEYQEIL GEIARLNRIL NDFEVLMGVV RGELVEIRDE FGDERRTDIV DARHDFNRED
LIPEQTVVLT VSRTGYAKTQ PISDYQAQKR GGKGRSATAM KEDDVIEHLL VTSTHAHIMC
FTNTGRVFGL RGFEIPLASR GSKGRPLVNL INLEPEESVT AILPVADLKD EQSFVFFATA
SGTVKRVALS QFANLRANGL RAIDLAEGDT LIGVAITDGE QEIMLFSNEG KAIRFKENSI
RTMSRIAKGV RGMRVNLLAG VDDEEPIDDD TDDADDGFAV SRVVSLVVVP ASGEILCACE
NGFGKRTAIE DYPTKGRGGK GVIAIKTSER NGQLVKAVAV TGEEDVILIS DKGTLVRTPV
AQIAIAGRNA QGVKLIRIMD EEVLVGMACV EHEDEESADE SIEPSDNETA VE
//
