ID A0A1V0GXK3_9RHOB Unreviewed; 892 AA.
AC A0A1V0GXK3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ECO:0000313|EMBL:QEU10434.1};
GN ORFNames=A6J80_12515 {ECO:0000313|EMBL:ARC38542.1}, FOB51_06980
GN {ECO:0000313|EMBL:QEU10434.1};
OS Paracoccus yeei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC38542.1, ECO:0000313|Proteomes:UP000191257};
RN [1] {ECO:0000313|Proteomes:UP000191257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ARC38542.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_252 {ECO:0000313|EMBL:ARC38542.1};
RA Campos J., Goldberg B., Tallon L., Sadzewicz L., Sengamalay N., Ott S.,
RA Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S., Geyer C.,
RA Nandy P., Hobson J., 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.
RN [3] {ECO:0000313|EMBL:QEU10434.1, ECO:0000313|Proteomes:UP000324507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_643 {ECO:0000313|EMBL:QEU10434.1,
RC ECO:0000313|Proteomes:UP000324507};
RA Sciortino C., Tallon L., Sadzewicz L., Vavikolanu K., Mehta A.,
RA Aluvathingal J., Nadendla S., Nandy P., Geyer C., Yan Y., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2019) 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; CP020442; ARC38542.1; -; Genomic_DNA.
DR EMBL; CP044081; QEU10434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0GXK3; -.
DR STRING; 147645.A6J80_12515; -.
DR KEGG; pye:A6J80_12515; -.
DR eggNOG; COG0188; Bacteria.
DR Proteomes; UP000191257; Chromosome.
DR Proteomes; UP000324507; 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; 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:UP000191257};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 8..487
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 548..554
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; 97979 MW; A4176A8FF61DC2E3 CRC64;
MPHDGPVIDI AREMRSSYLD YAMSVIVSRA IPDLRDGLKP VHRRILFAMH ETGNTHDKPY
RKSARPVGDV MGKYHPHGDA AIYDALVRMA QDFSMSLPLL DGQGNFGSMD GDSAAAMRYT
EVRMDKPSAY LLMDIDKDTV EFQDNYDGKD REPTVLPARF PNMLVNGAGG IAVGMATNIP
PHNLGEVIDA TLELIANPDL PTERLLDIIP GPDFPTGGII LGRSGARKAY LEGRGSVVIR
AKTRIEEGRN GRQMIVLDEI PYQVNKATLI EKIAELAKEK RIEGIAHVQD ESDRVGVRVV
IELKRDATAE VVLNQLFRFT AMQTSFGCNM LALNGGRPEQ LALRDFLTHF IAFREEVVAR
RTAYELRRAR ERAHVLCGLA VAVSNVDEVV ATIRSSADAA EARGRLMERR WPAHEIVEYL
RLIDDPLHPV NEDGTYNLSE TQARAILELR LQRLTQLGVQ EVTDELKSLA ESIRDYLAIL
ASRDRIMAII SDELREVRSQ FAVPRRTEIT DWAGDLDDED LIEREDMVVT ITSGGYIKRT
ALAEFRSQRR GGKGLSGMAT KEDDVVTTLF VANTHTELLF FTTDGMVYRL KTWRLPLGGR
TAKGKAIVNI LPIDPGVSIA ALMPVDAPEK DWEDYQVVFA TSDGDVRRNA LSDFANVMRN
GKIAMKLPEG VELIGVRMAT AGDDVMLVTA AGRAIRFPTT DVRVFKGRDS TGVRGIRLAK
GDRVVSMSVI RHFEADPAER AAYLKMRRAV AGALDDGAEA DEDEEAVAEG SVTQERYAEM
SAAEDLILTI TAKGSGKISS SHDYPVRGRG GQGVMAMDKA MRGGELVASF PVEGDDQIML
ATSTGQSIRV PVDGISFRSR SAGGVRVFNT GEGETVVSVA RIAENGEDEA EA
//
