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MUKB_SHIDS
ID   MUKB_SHIDS              Reviewed;        1483 AA.
AC   Q32E44;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-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=SDY_2334;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
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; CP000034; ABB62411.1; -; Genomic_DNA.
DR   RefSeq; WP_000572767.1; NC_007606.1.
DR   RefSeq; YP_403902.1; NC_007606.1.
DR   AlphaFoldDB; Q32E44; -.
DR   SMR; Q32E44; -.
DR   STRING; 300267.SDY_2334; -.
DR   EnsemblBacteria; ABB62411; ABB62411; SDY_2334.
DR   KEGG; sdy:SDY_2334; -.
DR   PATRIC; fig|300267.13.peg.2818; -.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   Proteomes; UP000002716; 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;
KW   Reference proteome.
FT   CHAIN           1..1483
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000069913"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          326..418
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          444..480
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          509..601
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          780..804
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          837..923
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          977..1115
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1209..1265
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   1483 AA;  169899 MW;  43BDADD0E653F422 CRC64;
     MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LKVGVCYSML DTINSRHQRV VVGVRLQQVA GRDRKVDIKP
     FAIQGLPMSV QPTQLVTETL NERQARVLPL NELKDKLEAM EGVQFKQFNS ITDYHSLMFD
     LGIIARRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRMTLEAIR VTQSDRDLFK HLISEATNYV AADYMRHANE RRVHLDKALE FRRELYTSRQ
     QLAAEQYKHV DMARELAEHN GAEGDLEADY QAASDHLNLV QTALRQQEKI ERYEADLDEL
     QIRLEEQNEV VAEAIERQEE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI
     AALNRAKELC HLPDLTADSA AEWLETFQAK ELEATEKMLS LEQKMSMAQT AHSQFEQAYQ
     LVVAINGPLA RNEAWDVARE LLREGVEQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA
     DFCKRQGKNF DIDELEALHQ ELEARIASLS DSVSNAREER MALCQEQEQL QSRIQSLMQR
     APVWLAAQNS LNQLSEQCGE EFSSSQDVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI
     ERLSQPGGSE DQRLNALAER FGGVLLSEIY DDVSLEDAPY FSALYGPSRH AIVVPDLSQV
     TEHLEGLTDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPEVPLFGR
     AACESRIESL HAEREVLSER FATLSFDVQK TQRLHQAFSR FIGSHLAVAF ESDPEPEIRQ
     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 NLTRKLRRLE RDYFEMREQV VTAKAGWCAV MRMVKDNGVE RRLHRRELAY
     LSADDLRSMS DKALGALRLA VADNEHLRDV LRMSEDPKRP ERKIQFFVAV YQHLRERIRQ
     DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRILNQ
     GLQNVSFGQV NSVRLNVNVR ETHAMLLDVL SEQHEQHQDL FNSNRLTFSE ALAKLYQRLN
     PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
     VVQSWEDESR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP
     EKGTTYKLVR KVFQNTEHVH VVGLRGFAPQ LPETLPGSDE APS
 
 
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