ID A0A071LV97_9ENTR Unreviewed; 1486 AA.
AC A0A071LV97;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-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:KEA52508.1};
GN ORFNames=DT73_10355 {ECO:0000313|EMBL:KEA52508.1};
OS Mangrovibacter sp. MFB070.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Mangrovibacter.
OX NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA52508.1, ECO:0000313|Proteomes:UP000027726};
RN [1] {ECO:0000313|EMBL:KEA52508.1, ECO:0000313|Proteomes:UP000027726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB070 {ECO:0000313|EMBL:KEA52508.1,
RC ECO:0000313|Proteomes:UP000027726};
RA Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT Bacterium Isolated from an Aquaculture Farm.";
RL Submitted (APR-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:KEA52508.1}.
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; JJMI01000022; KEA52508.1; -; Genomic_DNA.
DR RefSeq; WP_036107803.1; NZ_JJMI01000022.1.
DR eggNOG; COG3096; Bacteria.
DR Proteomes; UP000027726; 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}; Reference proteome {ECO:0000313|Proteomes:UP000027726}.
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 666..783
FT /note="Flexible hinge"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT REGION 989..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 343..426
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 515..600
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COMPBIAS 989..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1486 AA; 169493 MW; BA4140B166820C35 CRC64;
MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LKAGVCYSFL DVVNSRHQRV LVGVRLQQVA GRDRKVDIKP
FAIQGLPMAV QPTQLVTEAL NARQARVLTL QELKEKTEAM EGVQFRQFSS ITDYHALMFD
LGVVARRLRS ASDRSKYYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATDYV AADYMRHANE RRIHLDQALA TRQELFTSRK
QLATEQYRHV EMARELAEQA GAEGDLEADY QAASDHLNLV QTALRQQEKI ERYEADLEEL
QIRLEEQNEV VAEAQDLHEE HEARAEAAEL EVDELKNQLA DYQQALDVQQ TRALQYQQAL
QALNRARELC SLPDLTVDSA DEWLDTFQAK EQEGTETLLS LEQKMRVSQT AHAQFEEAWK
LVCAISGPVS RSDAWQVARD LLRDAADQRH QAEQVPALRM RLSELEQRLR EQQDAERLLA
EFSRQQGREV LPEELETWQE EFEAKIASLS ERVSQASEER SSLRQEHEQL QQKIQLLTQR
APVWLAAQSS LNQLSEQSGE EFTSGQEITE HLQQLLERER ENIVERDSVS ARKQAVDDEI
ERLSQPGGAE DARLNALAER FGGVLLSEIY DDVGLDDAPY FSALYGPSRH AIVVPELSRV
REYLDGLEDC PEDLYLIEGD PQSFDDSVFS VEELEKAVVV KIADRQWRYS RFPSVPLFGR
AARESRIESL HAEREELAEK FATLSFDVQK TQRLHQAFSR FIGQHLSVAF DDDPEAAIRQ
LNTRRSEIER TLSQHESDNQ QQKNQYEQAR EGVALLNRLL PRANLLGDET LADRVEEIQA
QVDEAQEAAR YLQQHGSQLA RLEPVASVLQ SDPEQFEQLK SDYENAKRTQ TEARQQAFAL
AEVVQRRAHF SYSDAVEILS GNSDLNEKLR QRLEQAESER SRSREALRSH GAQLNQYHQV
LASLKSSWET KNELLSDLHK ELQDIGVRAD AGAEERARTR RDELHNQLSG NRSRRNQLEK
QLTFCEAEMD NLTRALRRLE RSYHEIREQV VTAKAGWCAV MRLVKENGVE RRLHRRELAY
LSGDELRSMS DKALGALRQA VADNEHLRDV LRLSEDPKRP ERKIQFFVAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
GLQSVSFGQV NSVRLNVNIR EAHATLLDVL SEQHEQHQDL FNSQRLTFSE ALAKLYQRLN
PQIDMGQRTP QTIGEELLDY RNYLDMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEDESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCERLEMQL IIAAPENISP
EKGTTYKLMR KVTAQGEHVH VVGLRGFAPP LPEASQDAAP AASDAS
//
