ID A0A174HWY4_9CLOT Unreviewed; 840 AA.
AC A0A174HWY4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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_2 {ECO:0000313|EMBL:CUO77847.1};
GN Synonyms=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN ORFNames=DXC39_15020 {ECO:0000313|EMBL:RGM03336.1}, ERS852407_03936
GN {ECO:0000313|EMBL:CUO77847.1};
OS Hungatella hathewayi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=154046 {ECO:0000313|EMBL:CUO77847.1, ECO:0000313|Proteomes:UP000095651};
RN [1] {ECO:0000313|EMBL:CUO77847.1, ECO:0000313|Proteomes:UP000095651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608850 {ECO:0000313|EMBL:CUO77847.1,
RC ECO:0000313|Proteomes:UP000095651};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RGM03336.1, ECO:0000313|Proteomes:UP000261257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF05-11AC {ECO:0000313|EMBL:RGM03336.1,
RC ECO:0000313|Proteomes:UP000261257};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYZE01000011; CUO77847.1; -; Genomic_DNA.
DR EMBL; QSSQ01000014; RGM03336.1; -; Genomic_DNA.
DR RefSeq; WP_055657742.1; NZ_QSVU01000015.1.
DR AlphaFoldDB; A0A174HWY4; -.
DR Proteomes; UP000095651; Unassembled WGS sequence.
DR Proteomes; UP000261257; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000095651};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 12..470
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 810..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..469
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 531..537
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 824..840
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 840 AA; 94581 MW; 4AE66FB57C356CEB CRC64;
MEPNIFDKVH EVDLKKTMEK SYIDYAMSVI AARALPDVRD GLKPVQRRVL FSMIELNNGP
DKPHRKCARI VGDTMGKYHP HGDSSIYGAL VNMAQEWSTR YPLVDGHGNF GSVDGDGAAA
MRYTEARLSK VSMEMLADIG KNTVDFTPNF DETEKEPVVL PARFPNLLVN GTSGIAVGMA
TNIPPHNLRE VIGAVVKVID NQVEENRETE MEEVLEIIKG PDFPTGATIL GKMGIEEAYR
TGRGKIRVRA VTDIETLPNG KSRIIVTELP YMVNKARLIE KMAELAKEKK IDGITDLRDE
SDRTGMRIVI ELRRDVNANV ILNQLLKHTQ LQDTFGVIML ALVNNEPRVL NLMQMLKLYL
EHQKEVVTRR TQYDLNKAEE RAHILQGLLI ALDNIDEVIR IIRNSQNVQI AKAELMERFG
LSDVQSQAIV DMRLRALTGL EREKLENEFK ELEAKIEELR AILADEKKLL GVIREEIMLI
SDKYGDDRRT SIGFDEFDMS MEDLIPDEST IVAMTKLGYI KRMSVDNFRS QNRGGKGIKG
MQTIDQDYIE DLIMTTNHHY IMFFTNTGRV YRLKTYAIPE GSRTARGTAI INLLQLLPGE
SITAIIPMKE YDDDKFLFMA TKNGMVKKTP MMEYANVRKN GLQAIVLRED DELIEVKATD
NSKDIFLITK MGQCIRFNET DVRVTGRVSM GVIGMKLNDD DEVVGMQMDT QGEKLLIVSE
NGMGKRTPID EFTPQKRGGK GVLCYKITEK TGMIVGAKLV HDDHDIMIIT NEGIVIRITV
EDISVIGRNT SGVKLMNIDQ ESDIRVASIA KVRDDGSKSE GEGMEDLDLE DEETAPETEE
//
