(data stored in ACNUC7421 zone)

HOGENOM: ECO26_1_PE1002

ID   ECO26_1_PE1002                       STANDARD;      PRT;   1486 AA.
AC   ECO26_1_PE1002; C8TM39;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Chromosome partition protein mukB;AltName: Full=Structural
DE   maintenance of chromosome-related protein; (ECO26_1.PE1002).
GN   Name=mukB; OrderedLocusNames=ECO26_1050;
OS   ESCHERICHIA COLI O26:H11 STR. 11368.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=573235;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECO26_1.PE1002.
CC       Escherichia coli O26:H11 str. 11368, complete genome.
CC       1..66570 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:C8TM39_ECO26
CC   -!- FUNCTION: Plays a central role in chromosome condensation,
CC       segregation and cell cycle progression. Functions as a homodimer,
CC       which is essential for chromosome partition. Involved in negative
CC       DNA 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 (By similarity).
CC   -!- SUBUNIT: Homodimerization via its hinge domain. Binds to DNA via
CC       its C-terminal region. Interacts, and probably forms a ternary
CC       complex, with mukE and mukF via its C-terminal region. The complex
CC       formation is stimulated by calcium or magnesium. Interacts with
CC       tubulin-related protein ftsZ (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid. Note=Restricted to the
CC       nucleoid region (By similarity).
CC   -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC       coiled coil regions, allows the homodimerization, forming a V-
CC       shaped homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the SMC family. MukB subfamily.
CC   -!- GENE_FAMILY: HOG000278243 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C8TM39; -.
DR   EMBL; AP010953; BAI24366.1; -; Genomic_DNA.
DR   RefSeq; YP_003228106.1; NC_013361.1.
DR   STRING; C8TM39; -.
DR   EnsemblBacteria; EBESCT00000175586; EBESCP00000161689; EBESCG00000174935.
DR   GeneID; 8481895; -.
DR   GenomeReviews; AP010953_GR; ECO26_1050.
DR   KEGG; eoj:ECO26_1050; -.
DR   GeneTree; EBGT00050000010344; -.
DR   ProtClustDB; PRK04863; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:HAMAP.
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:HAMAP.
DR   GO; GO:0006260; P:DNA replication; IEA:HAMAP.
DR   HAMAP; MF_01800; MukB; 1; -.
DR   InterPro; IPR012090; MukB.
DR   InterPro; IPR007406; Scp_MukB_N.
DR   Gene3D; G3DSA:3.40.1140.10; Scp_MukB_N; 1.
DR   Pfam; PF04310; MukB; 1.
DR   PIRSF; PIRSF005246; MukB; 1.
DR   HOGENOMDNA; ECO26_1.PE1002; -.
KW   cell division protein MukB;
KW   ATP-binding; Cell cycle; Cell division; Chromosome partition;
KW   Coiled coil; Complete proteome; Cytoplasm; DNA condensation;
KW   DNA-binding; Nucleotide-binding.
SQ   SEQUENCE   1486 AA;  UNKNOWN MW;  UNKNOWN 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 QTALRQQEKI ERYEADLDEL
     QIRLEEQNEV VAEAIERQEE NEARAEAAEL EVDELKSQLA NYQQALDVQQ TRAIQYNQAI
     AALNRAKELC HLPDLTADSA AEWLETFQAK ELEATEKMLS 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 AIVVPDLSQI
     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 MRMVKDNGVE 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 APSQAS
//

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