ID A0A263HBL2_9PAST Unreviewed; 1519 AA.
AC A0A263HBL2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:SUU36750.1};
GN ORFNames=NCTC10851_01331 {ECO:0000313|EMBL:SUU36750.1};
OS Actinobacillus seminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=722 {ECO:0000313|EMBL:SUU36750.1, ECO:0000313|Proteomes:UP000254507};
RN [1] {ECO:0000313|EMBL:SUU36750.1, ECO:0000313|Proteomes:UP000254507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10851 {ECO:0000313|EMBL:SUU36750.1,
RC ECO:0000313|Proteomes:UP000254507};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; UFSB01000001; SUU36750.1; -; Genomic_DNA.
DR InParanoid; A0A263HBL2; -.
DR OrthoDB; 6722439at2; -.
DR Proteomes; UP000254507; 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; 1.
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 52..276
FT /note="MukB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04310"
FT DOMAIN 695..860
FT /note="MukB hinge"
FT /evidence="ECO:0000259|Pfam:PF16330"
FT REGION 716..833
FT /note="Flexible hinge"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 358..513
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 564..643
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 888..965
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 1027..1061
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 1130..1157
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT BINDING 84..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1519 AA; 173750 MW; 73310BC0C48AB2D2 CRC64;
MSDIFEQENE ILDLEKGIIA NDIDEMSLEK ADLETYSVTM SQFNPALQSV GVERGKFRSL
TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAGFVTA LIPDLTLLHF RNTTEAGSTG
GSRDKGLHGK LRPGVCYAAL DTINSRHQRI VVGVRLQQVA GRDKKVDIKT FSIQGLELSL
NPTAVFTETV GERQARVLNL NELKDKIENL GAQFKQYPSI TDYHGMMFDL GIIPKRLRSS
SDRSKFYKLI EASLYGGISS AITKSLRDYL LPENLGVRKA FQDMESALRE NRMTLEAIKV
TQADRDLFKH LITETTNYVA SDYMRNANER LGNIQTALSF RQDWYKAKAE QDLSQHRLID
LSREAAELAE NEKMLEADHQ SAVDHLNLVL NALRHQEKIS RYHENVATLR EKLEEQKMAV
EEANEQQEAS QAQLDQVELE ADQLRNQLAD YQQALDAQQT RALQYNQAIS ALEKAKYLCG
LAELSVKNVE DYYAEFEAQA EDITAKVLEL EQKMSISEAA KTQFDKAYQL VCSIAGEMPR
SAAWESAKTL LREYPRQKVQ AQQSASLRGK LHELEQRYAQ QQSAVRLLKD VNQRANLALE
SVEELEDFYA EQEALADDLS AELSEQVEQR STLRQKREQL TALYEENARK APAWLAAQAA
LERLQEQSGA NFADSQDVMN FMQAQLVKER EFTIERDQLE QKRQHLDEQI SRLSQPDGSE
DPRLNALAES FGGVLLSELY DDVPIEDAPY FSALYGPARH AIVVRDLTAV KEQLSQLEDC
PEDLYLIEGD PAEFDDSVFN AQELELGVVV QVSNREVRYS KFPEIPLFGR AAREKRLEEL
QAQRDEIAEQ YAQRAFDVQK CQRLHEHFSQ FVGLHLALAF LPNPETLMAE VQRERNEIER
ELNQFSSGEQ QIRMQLDNAK EKMQLLNKLL PQVNVLADET LMDRIEECRE QLDEAEQAAH
FIRQYGNALA QLEPIANTLQ SDPENYERLK ADYESAVGLQ KQIQQRVFAL ADVVQRKAHF
SYEDTVKSET SELNEQLRQR LEQVQKQREQ QREIVRQKQV RFAQYNQVYI ELRSSFDEKN
KMLNELIGEI GQLGVCADDG AEERARIRRD ELYQQLSTGR QRRTYIEKQL TQIETESENL
TRRIRKAERD YKTQRELVVA AKVSWCVVLR LSRNSDVEKR LNRRELAYLS ADDLRSMSDK
ALGALRTAVA DNEYLRDALR ISEDSRKPEN KVRFFIAVYQ HLRERIRQDI IKTDDPIDAI
EQMEIELSRL TSELTGREKK LAISSESVAN IMRKTIQREQ NRIRMLNQGL QNIAFGQVKS
VRLVVNIRDT HAMLLDALSG NQAEYQDLFS DNRMTFSEAM AKLYQRINPH IDMGQRTAQT
IGEELLDYRN YLDLEVEVYR GADGWLRAES GALSTGEAIG TGMSILLMVV QSWEEESRRI
RGKDIVPCRL LFLDEAARLD AKSISTLFEL CERLDMQLLI AAPENISPEK GTTYKLVRKI
SGNQEHVHVV GLRGFGATE
//
