MUKB_SALHS
ID MUKB_SALHS Reviewed; 1488 AA.
AC B4TDR1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Chromosome partition protein MukB {ECO:0000255|HAMAP-Rule:MF_01800};
DE AltName: Full=Structural maintenance of chromosome-related protein {ECO:0000255|HAMAP-Rule:MF_01800};
GN Name=mukB {ECO:0000255|HAMAP-Rule:MF_01800}; OrderedLocusNames=SeHA_C1092;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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:0000255|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:0000255|HAMAP-Rule:MF_01800}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC Rule:MF_01800}. Note=Restricted to the nucleoid region.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01800}.
CC -!- SIMILARITY: Belongs to the SMC family. MukB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01800}.
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DR EMBL; CP001120; ACF69556.1; -; Genomic_DNA.
DR RefSeq; WP_000572753.1; NC_011083.1.
DR AlphaFoldDB; B4TDR1; -.
DR SMR; B4TDR1; -.
DR KEGG; seh:SeHA_C1092; -.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR Proteomes; UP000001866; Chromosome.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
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; 3.30.70.3500; -; 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 Pfam; PF04310; MukB; 1.
DR Pfam; PF16330; MukB_hinge; 1.
DR PIRSF; PIRSF005246; MukB; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Chromosome partition; Coiled coil;
KW Cytoplasm; DNA condensation; DNA-binding; Nucleotide-binding.
FT CHAIN 1..1488
FT /note="Chromosome partition protein MukB"
FT /id="PRO_1000187485"
FT REGION 666..783
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT REGION 1049..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 326..418
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 444..472
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 509..602
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 835..923
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 977..1116
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1209..1265
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COMPBIAS 1049..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:0000255|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1488 AA; 170088 MW; FC5F482B9B88489A CRC64;
MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LKAGVCYSML DTINSRHQRV VVGVRLQQVA GRDRKVDIKP
FAIQGLPMSV QPTQLVTETL NERQARVLSL AELKDKLDEM EGVQFKQFNS ITDYHSLMFD
LGIIARRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
ENRLTLEAIR VTQSDRDLFK HLISEATDYV AADYMRHANE RRVHLDQALA FRRELYTSRK
QLAAEQYKHV DMARELGEHN GAEGSLEADY QAASDHLNLV QTALRQQEKI ERYEADLEEL
QIRLEEQNEV VAEAAEMQDE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI
SALSRAKELC HLPDLTPESA AEWLDTFQAK EQEATEKLLS LEQKMSVAQT AHSQFEQAYQ
LVAAINGPLA RSEAWDVARE LLRDGVNQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA
EFCKRQGKNF DIDELEALHQ ELEARIASLS DSVSSASEQR MALRQEQEQL QSRIQHLMRR
APVWLAAQNS LNQLSEQCGE EFTSSQEVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI
ERLSQPGGAE DQRLNALAER FGGVLLSEIY DDVSLEDAPY FSALYGPSRH AIVVPDLSQI
AEQLEGLTDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPSLPIFGR
AARENRIESL HAEREVLSER FATLSFDVQK TQRLHQAFSR FIGSHLSVAF EDDPEAEIRR
LNGRRVELER ALATHESDNQ QQRLQFEQAK EGVSALNRLL PRLNLLADET LADRVDEIQE
RLDEAQEAAR FVQQYGNQLA KLEPVVSVLQ SDPEQFEQLK EDYAWSQQMQ RDARQQAFAL
AEVVERRAHF SYSDSAEMLS GNSDLNEKLR QRLEQAEAER TRAREALRSH AAQLSQYSQV
LASLKSSYDT KKELLNDLQR ELQDIGVRAD SGAEERARQR RDELHAQLSN NRSRRNQLEK
ALTFCEAEME NLTRKLRKLE RDYHEMREQV VTAKAGWCAV MRMVKDNGVE RRLHRRELAY
LSADELRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKIQFFVAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
GLQSVSFGQV NSVRLNVNVR ETHATLLDVL SEQQEQHQDL FNSNRLTFSE ALAKLYQRLN
PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEDEAR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP
EKGTTYKLVR KVFQNTEHVH VVGLRGFAPQ LPETLPGTQT EDTPSEAS
