ID A0A014PS90_9GAMM Unreviewed; 1487 AA.
AC A0A014PS90;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chromosome partition protein MukB {ECO:0000256|HAMAP-Rule:MF_01800};
DE AltName: Full=Structural maintenance of chromosome-related protein {ECO:0000256|HAMAP-Rule:MF_01800};
GN Name=mukB {ECO:0000256|HAMAP-Rule:MF_01800,
GN ECO:0000313|EMBL:EXU73707.1};
GN ORFNames=BG55_21065 {ECO:0000313|EMBL:EXU73707.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU73707.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU73707.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU73707.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a central role in chromosome condensation, segregation
CC and cell cycle progression. Functions as a homodimer, which is
CC essential for chromosome partition. Involved in negative DNA
CC supercoiling in vivo, and by this means organize and compact
CC chromosomes. May achieve or facilitate chromosome segregation by
CC condensation DNA from both sides of a centrally located replisome
CC during cell division. {ECO:0000256|HAMAP-Rule:MF_01800}.
CC -!- SUBUNIT: Homodimerization via its hinge domain. Binds to DNA via its C-
CC terminal region. Interacts, and probably forms a ternary complex, with
CC MukE and MukF via its C-terminal region. The complex formation is
CC stimulated by calcium or magnesium. Interacts with tubulin-related
CC protein FtsZ. {ECO:0000256|HAMAP-Rule:MF_01800}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000256|HAMAP-
CC Rule:MF_01800}. Note=Restricted to the nucleoid region.
CC {ECO:0000256|HAMAP-Rule:MF_01800}.
CC -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the homodimerization, forming a V-shaped
CC homodimer. {ECO:0000256|HAMAP-Rule:MF_01800}.
CC -!- SIMILARITY: Belongs to the SMC family. MukB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01800}.
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:EXU73707.1}.
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DR EMBL; JFHN01000074; EXU73707.1; -; Genomic_DNA.
DR RefSeq; WP_034941138.1; NZ_JFHN01000074.1.
DR STRING; 69222.BG55_21065; -.
DR PATRIC; fig|69222.5.peg.4301; -.
DR OrthoDB; 6722439at2; -.
DR Proteomes; UP000019918; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0009295; C:nucleoid; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.58.850; -; 1.
DR Gene3D; 3.40.1140.10; -; 2.
DR Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1.
DR Gene3D; 3.30.70.3500; MukB, hinge domain; 1.
DR HAMAP; MF_01800; MukB; 1.
DR InterPro; IPR012090; MukB.
DR InterPro; IPR032520; MukB_hinge.
DR InterPro; IPR042501; MukB_hinge_sf.
DR InterPro; IPR007406; MukB_N_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42963; CHROMOSOME PARTITION PROTEIN MUKB; 1.
DR PANTHER; PTHR42963:SF1; CHROMOSOME PARTITION PROTEIN MUKB; 1.
DR Pfam; PF04310; MukB; 1.
DR Pfam; PF16330; MukB_hinge; 1.
DR Pfam; PF13558; SbcC_Walker_B; 1.
DR PIRSF; PIRSF005246; MukB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01800};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01800}; Reference proteome {ECO:0000313|Proteomes:UP000019918}.
FT DOMAIN 2..227
FT /note="MukB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04310"
FT DOMAIN 645..810
FT /note="MukB hinge"
FT /evidence="ECO:0000259|Pfam:PF16330"
FT REGION 639..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..783
FT /note="Flexible hinge"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 343..412
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 508..600
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 838..1109
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1487 AA; 170161 MW; F0ED82454411E7DA CRC64;
MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFITA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LRPGVCYAAL DVINSVHQRV IVGVRLQQVA GRDRKVDIKP
FSIHGLPTSL NPTEVLTETV NARQARVLPL SELKEKFEAM ESVQFRQFNS ITDYHSLMFD
LGIVARRLRS AADRSKYYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATSYV AADYMRHANE RRIHLDGALQ QRGELFGSRR
QLATEQYRHV EMARELGEHN GAESDLETDY QSASDHLNLV QTAMRQQEKI ERYEGDIDEL
TYRLEEQNEV VAEAREVQEE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
AALQRAQQVC QIPDLNVDNA ESWQETFRAK EQEATDKLLM LEQKMSVADA AHGQFAQAFD
LVTRIAGPVS RSDAWQTGRD LLRDASNQRY HAEQLQSLRA RLSELEQRLR EQQDAERLLN
EFSKRHGQQY HPQELEALQH ELEAQIELLS ESVSEAGEKR MNLRQELDQV REQIARLTRL
APQWLAAQDI LTQLSEQTGQ SLESSQQVTE FMQQLLERER ETTVERDEVS SRKRDVEKQI
ERLSQPGGAE DGRLNNLAER FGGVLLSEIY DDVTIDDAPY FSALYGPARY AIVVPDLSLV
RDLLDGLEDC PEDLYLIEGD PQSFDDSVFS VEELQKAVVV KAGDRQWRYS RFPKVPLFGR
AARENQLERL HAERETLAER FATLSFDVQK TQRLHQSFSR FIGSHLAVAF EPDPEAQIRI
LNSRRGELER ALSAHESENQ QQRQQFDQAK EGVAQLNRLM PRVSLLLDET LQDRYEEILE
RLDEAQEAAR FLQQHGQHLA KLEPIVAVLQ NDPEQHDQLK QDYQQAQLIQ RDARQQAFAV
TEVVQRRAHF SYVDSAGMLD GNSDLNEKLR HRLEQVESER ARAREQLRTH QAQLTQYSQV
LASLKSSFDA KQDMLKELQQ EMQDIGVQAD ASAEERARLR RDELYSALSN NRARRNQLEK
QLTFCEAEMD ALQKKLKRVE RDYHQNREQV VSAKAGWVAV LRMVKDNGVE RRLHRRELAY
LGGDELRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKIQFFIAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELG RLTEELTARE QMLAISSRSV SNIIRKTIQR EQNRIRQLNQ
GLQSVSFGQV HSVRLNVNVR ESHAMLLDVL SEQHEQHQDL FNSNRLTFSE ALAKLYQRLN
PQIDMGQRMP QTIGEELLDY RNYLDMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEEESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCDRLEMQL IIAAPENISP
EKGTTYKLVR KVINNTEHVH VVGLRGFAAE PSTISSDDIA DGQSVAG
//
