MUKB_SHISS
ID MUKB_SHISS Reviewed; 1486 AA.
AC Q3Z3J7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=SSON_0926;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87665.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z3J7; -.
DR SMR; Q3Z3J7; -.
DR EnsemblBacteria; AAZ87665; AAZ87665; SSON_0926.
DR KEGG; ssn:SSON_0926; -.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR Proteomes; UP000002529; 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..1486
FT /note="Chromosome partition protein MukB"
FT /id="PRO_1000069915"
FT REGION 666..783
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 334..418
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 444..480
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 509..603
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 835..923
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 977..1115
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1209..1266
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1486 AA; 170331 MW; 0A179A7A5B5F637F CRC64;
MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LKAGVCYSML DTINSRHQRV VVGVRLQQVA GRDRKVDIKP
FAIQGLPMSV QPTQLVTETL NERQARVLPL NELKDKLEAM EGVQFKQFNS ITDYHSLMFD
LGIIARRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATNYV AADYMRHANE RRVHLDKALE FRRELHTSRQ
QLAAEQYKHV DMARELAEHN GAEGDLEADY QAASDHLNLV QTAQRQQEKI ERYEADLDEL
QIRLEEQNEV VAEAIERQEE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI
AALNRAKELC HLPDLTADSA AEWLETFQAK EQEATEKMLS LEQKMSMAQT AHSQFEQAYQ
LVVAINGPLA RNEAWDVARE LLREGVDQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA
DFCKRQGKNF DIDELEALHQ ELEARIASLS DSVSNAREER MALRQEQEQL QSRIQSLMQR
APVWLAAQNS LNQLSEQCGE EFTSSQDVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI
ERLSQPGGSE DQRLNALAER FGGVLLSEIY DDVSLEDAPY FSALYGPSRH AIVVPDLSQV
TEHLEGLTDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPEVPLFGR
AARESRIESL HAEREVLSER FATLSFDVQK TQRLHQAFSR FIGSHLAVAF ESDPEAEIRQ
LNSRRVELER ALSNHENDNQ QQRIQFEQAK EGVTALNRIL PRLNLLADDS LADRVDEIRE
RLDEAQEAAR FVQQFGNQLA KLEPIVSVLQ SDPEQFEQLK EDYAYSQQMQ RDARQQAFAL
TEVVQRRAHF SYSDSAEMLS GNSDLNEKLR ERLEQAEAER TRAREALRGH AAQLSQYNQV
LASLKSSYDT KKELLNDLQR ELQDIGVRAD SGAEERARIR RDELHAQLSN NRSRRNQLEK
ALTFCEAEMD NLTRKLRKLE RDYFEMREQV VTAKAGWCAV MRMVKDNVVE RRLHRRELAY
LSADDLRSMS DKALGALRLA VADNEHLRDV LRMSEDPKRP ERKIQFFVAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
GLQNVSFGQV NSVRLNVNVR ETHAMLLDVL SEQHEQHQDL FNSNRLTFSE ALAKLYQRLN
PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEDESR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP
EKGTTYKLVR KVFQNTEHVH VVGLRGFAPQ LPETLPGSDE APSQES
