ID A0A3N4WKN5_9PAST Unreviewed; 1486 AA.
AC A0A3N4WKN5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=EDC49_0655 {ECO:0000313|EMBL:RPE96266.1};
OS Frederiksenia canicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Frederiksenia.
OX NCBI_TaxID=123824 {ECO:0000313|EMBL:RPE96266.1, ECO:0000313|Proteomes:UP000276901};
RN [1] {ECO:0000313|EMBL:RPE96266.1, ECO:0000313|Proteomes:UP000276901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25797 {ECO:0000313|EMBL:RPE96266.1,
RC ECO:0000313|Proteomes:UP000276901};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-2018) 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:RPE96266.1}.
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; RKQT01000001; RPE96266.1; -; Genomic_DNA.
DR OrthoDB; 6722439at2; -.
DR Proteomes; UP000276901; 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; 1.20.58.850; -; 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}.
FT DOMAIN 21..245
FT /note="MukB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04310"
FT DOMAIN 665..829
FT /note="MukB hinge"
FT /evidence="ECO:0000259|Pfam:PF16330"
FT REGION 685..802
FT /note="Flexible hinge"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 334..444
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 526..619
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 857..927
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 1003..1126
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1486 AA; 170471 MW; 1A1A21EFA5EDBB05 CRC64;
MEQVALQNNQ IIAPLARPEG VARGKFRSLT LINWNGFFAR TFDLDELVTT LSGGNGAGKS
TTMAGFVTAL IPDLSLLNFR NTTEAGSTSS SRDKGLYGKL KAGVCYAVLE SENSRKQRIM
TGVRLQQIAG RDKKVDIRSF SIQNIEENQS VISILTEQVG EKNARVLPLN ELKDKFDGTA
VQFKQYNSIT DYHSFLFDLG VIPKRLRSSS DRSKFYKLIE ASLYGGISSV ITKSLRDYLL
PENTGVRQAF QDMESALREN RMTLEAIKVT QSDRDMFKKL ITESTNYVSA DYMRNANERR
GNVQSAIEKR QEWYQAKSKI ELEQQRFVEF SREVKELGEA EAELETEYHN ANHQLNLVMN
AFRHQEKVER YQDEVEELAS KLEEQQMAVE EVAEKVEQVQ ARADEADDLV EDLRSQMADY
QQALDAQQTR ALQYQQAVNA LEKAKQLCGL PQLDLHNVED YHAEFAAQAD EITDNVFDLE
QRLAVSDMAK TQFDKAYELV CKIVGETDRL QADSVARELL SNFPSQKSQA QQAVVLRQKL
AELEQRLHQQ QHADRLLAEF NQKAQLQLAT ADDLESYYDE QQARVENVEA ELAELLDQRS
TQRQQREQFN QQYQQLAQNA PAWHTAQSAL SRLQEQCGET FTSSQAVMQA MQNTLSRERE
ATLARDELAR REQLLDEQIS RLSQPDGAED SRLNHLAEKF GGVLLSELYD DVSLEDAPYF
SALYGEARHA IVVRDLEATK AQLSQLDDCP DNLYLIEGDP NAFDDNVFPV EELGDGVVVQ
LSNRQWRYSK FSEFAVFGRA SREKQLEKLK IERDETAEKH AERAFDVQKC QRLHQHLSQF
IGTHLALAFQ PDPEVVMQQL SQQRNDIERE LAAASSQEQQ LRHQLESSKT QLQLLNKVLP
QLSLLADDTL QDRVEECREQ LLEAQDDEQF IRQYGNYLTQ LEPIAAALRS DPHQFEQLQA
DYKRSVEQQK LLNQKVFSLA DVMQRRLHFS YQETVGTEGP ALNEQLRQRV ENAQREREHY
KTQLRQAQSQ LTEYNQVFTA LRSSYDAKNQ MLQELLREMD EYGIRNDPEA VERATARRDE
IQQRLSQQRS RKHYLDKQLA VIEAEMDNLT KAVRKAERDY HAQREIVVQA KVSWCLVLKL
SRNSDVEKRL NRRELAYQSA EELRSISDKA LGALRQAVAD NEYLRDSLRA SEDSRKPENK
VAFFISVYQH LRERIRQDII KTDDPIDAIE QMEIELSRLT NELTSREKKL AISAESVANI
LRKTIQREQN RILQLNQGLQ NIAFGQVKGV RLVVNIRDTH AILLNALSQR EENSDLFDNA
KLSFSEALAM LYKRVNPHIE MGQRTPQTIG EELLDYRNYL DLEVETFRGA DGWMRAESSA
LSTGEAIGTG MSILLMVVQS WEEESRRLRA KDILPARLLF LDEAARLDAT SINTLFELCE
RLDMQLLIAA PENISPERGT TYKLVRKIAN NQEYVHVVGL KGFGQA
//
