MUKB_VIBCM
ID MUKB_VIBCM Reviewed; 1491 AA.
AC C3LN37;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=VCM66_1654;
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP001233; ACP05963.1; -; Genomic_DNA.
DR RefSeq; WP_000572788.1; NC_012578.1.
DR AlphaFoldDB; C3LN37; -.
DR SMR; C3LN37; -.
DR EnsemblBacteria; ACP05963; ACP05963; VCM66_1654.
DR GeneID; 57740366; -.
DR KEGG; vcm:VCM66_1654; -.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR Proteomes; UP000001217; Chromosome I.
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..1491
FT /note="Chromosome partition protein MukB"
FT /id="PRO_1000187491"
FT REGION 667..784
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT REGION 1059..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..450
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 490..600
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 836..1109
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1210..1239
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 1491 AA; 169960 MW; A515AAC8A761A011 CRC64;
MIERGKYQSL TMINWNGFFA RTFDIDNLVT TLSGGNGAGK STTMAAFITA LIPDQSLLHF
RNTTEAGSSQ ASRDKGLYGK LQAGACYAAL DVVNSRNQRL LFAVKLQQVA GRDKKVDIKP
FLIQGLPSHV KPTDVLVETV SDKHARVRQI NEVKDAVGQI EGAHFKSFPS IVDYHAQMFE
FGVIPKKLRN SSDRSKFYRL IEASLYGGIS SAITRSLRDY LLPQNGGVKK AFQDMESALR
ENRMTLEAIK TTQADRDLFK HLITESTNYV AADYMRHAND RRNKVGQTLV LRGELFSSRE
TLIEQNSLLN RVHEELELLV EQESALEQDY QGASDHLQLV QNALRQQEKI ERYQEDLEEL
NFRLEEQMMV VEEANERVMQ AEERAIISEE EVDSLKSQLA DYQQALDVQQ TRALQYQQAV
QALDKARRLL DKSELTAESA QALATQLKAE QETRTSELLA LKHKLDMSSA AAQQFNHAFE
LVKRVLGEVA RSEAAKQAQQ VIRQAREAQN VVQNEAQWQA QQRDLERQLE QQRSVRELAT
QYHKQHRVVL DDAATVELER ERHSALLEEL ETEQENCREQ RGQLRHQEQE LQTQIARFES
IAPAWIKAND ALETLREQSG AELADSQSVM AHMQQVLELE KAQSMAKDKL AERRTKLDSE
IERLASPGGS NDPRLKGLAD TLGGVLLSEI YDDITIDDAP YFSAMYGPAR HAIVVSDLSG
IKEKLVELDD CPEDLYLIEG DVDAFDDSSF NAEELEGAVC VQLNQRQMRY SRFPAIPLFG
RAAREQRLEL LREERDDVVE QHAKASFDSQ KLQRLYASFN QFVAMHLQVA FDADPEQALA
TARDKRNQLL RSISEFEAQE QQLRSQLQAS KQALAALDKL APQMGLLDEE TLEARYHELE
EKLQQLSEAK AFIAAHGRTI SELEKVAAVL DADPEQFDAL EQQYQQADQA LQQLKAQIFA
LSDLLERRHH FAYSDSVDLL NQSSELSEQL KAKLVQAESE RTRSREELKQ AQAQLSQYNQ
LLASLKSSHQ AKLETVQEFK QELQEFGVHA DEGAIERAQR RRDELQERLH TSRSRKSEYE
RTITSTELEM KALVKRMKKV EKDYQDLRTF VVNAKAGWCS VLRLARQNDV ERRLHKRELA
YLSADELRSM SDKSLGALRL AVANNEDLRD ALRQSEDNSR PERKVLFYIA VYQHLRERIR
QDIIRTDDPV EAIEEMEVEL ARLTEELTQR EQRLAISSDS VASIIRKTIQ REQNRIRMLN
QGLSNISFGQ VNGVRLNVKV RESHEILLAG LSEQQAQHKD LFESARYTFS EAMAKLFQRV
NPHIDMGQRS PQVLGEELLD YRNYLELSVE VNRGSDGWLQ AESGALSTGE AIGTGQSILL
MVVQSWEEES RRLRSKDIVP CRLLFLDEAA RLDAKSIATL FELCERLDMQ LLIAAPENIS
PEKGTTYKLV RKVFKDHEHV HVVGLRGFAQ TEKPKTAEQK FAEELAGELT E