ID D2YJ44_VIBMI Unreviewed; 1491 AA.
AC D2YJ44;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Chromosome partition protein MukB {ECO:0000256|HAMAP-Rule:MF_01800};
DE AltName: Full=Structural maintenance of chromosome-related protein {ECO:0000256|HAMAP-Rule:MF_01800};
GN Name=mukB {ECO:0000256|HAMAP-Rule:MF_01800,
GN ECO:0000313|EMBL:EEW05233.1};
GN ORFNames=VMB_35410 {ECO:0000313|EMBL:EEW05233.1};
OS Vibrio mimicus VM603.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=671074 {ECO:0000313|EMBL:EEW05233.1, ECO:0000313|Proteomes:UP000004827};
RN [1] {ECO:0000313|EMBL:EEW05233.1, ECO:0000313|Proteomes:UP000004827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM603 {ECO:0000313|EMBL:EEW05233.1,
RC ECO:0000313|Proteomes:UP000004827};
RX PubMed=19860885; DOI=10.1186/1471-2148-9-258;
RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T.,
RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.;
RT "Genomic taxonomy of Vibrios.";
RL BMC Evol. Biol. 9:258-258(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_01800}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000256|HAMAP-
CC Rule:MF_01800}. Note=Restricted to the nucleoid region.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01800}.
CC -!- SIMILARITY: Belongs to the SMC family. MukB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01800}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEW05233.1}.
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DR EMBL; ACYU01000186; EEW05233.1; -; Genomic_DNA.
DR RefSeq; WP_000572772.1; NZ_ACYU01000186.1.
DR Proteomes; UP000004827; Unassembled WGS sequence.
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: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; 1.20.58.850; -; 1.
DR Gene3D; 3.40.1140.10; -; 2.
DR Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1.
DR Gene3D; 3.30.70.3500; MukB, hinge domain; 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 PANTHER; PTHR42963; CHROMOSOME PARTITION PROTEIN MUKB; 1.
DR PANTHER; PTHR42963:SF1; CHROMOSOME PARTITION PROTEIN MUKB; 1.
DR Pfam; PF04310; MukB; 1.
DR Pfam; PF16330; MukB_hinge; 1.
DR Pfam; PF13558; SbcC_Walker_B; 1.
DR PIRSF; PIRSF005246; MukB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01800};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01800};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01800}.
FT DOMAIN 2..227
FT /note="MukB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04310"
FT DOMAIN 646..811
FT /note="MukB hinge"
FT /evidence="ECO:0000259|Pfam:PF16330"
FT REGION 667..784
FT /note="Flexible hinge"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT REGION 1059..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 309..412
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 515..590
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1491 AA; 169957 MW; 248DB7620297974A CRC64;
MIERGKYQSL TMINWNGFFA RTFDIDNLVT TLSGGNGAGK STTMAAFITA LIPDQSLLHF
RNTTEAGSSQ ASRDKGLYGK LQAGACYAAL DVVNSRNQRL LFAVKLQQVA GRDKKVDIKP
FLIQGLPSHV KPTDVLIETV SDKHARVRQI NEVKDAVGQI EGAHFKSFPS IVDYHAQMFE
FGVIPKKLRN SSDRSKFYRL IEASLYGGIS SAITRSLRDY LLPQNGGVKK AFQDMESALR
ENRMTLEAIK TTQADRDLFK HLITESTNYV AADYMRHAND RRNKVGQTLV LRGELFSSRE
TLIEQNSLLN RVHEELELLV EQESALEQDY QGASDHLQLV QNALRQQEKI ERYQEDLEEL
NFRLEEQMMV VEEANERVMM AEERATISEE EVDSLKSQLA DYQQALDVQQ TRALQYQQAV
QALDKARRLL DKPELTAESA QALATQLKAE QETRTSELLA LKHKLDMSSA AAQQFNHAFE
LVKRVLGEVA RSEAANQAQQ VIRQARDAQH VVQNEAQWQA QQRDLERQLE QQRSVRELAT
QYHKQHMVVL DDAATVELER ERHSALLEEL ETKQENCREQ RGQLRHQEQE LQTQIARFES
IAPAWIKAND ALETLREQSG AELADSQSVM AHMQQVLELE KAQSMAKDKL AERRTKLDSE
IERLASPGGS NDPRLKGLAD TLGGVLLSEI YDDITIDDAP YFSAMYGPAR HAIVVSDLSG
IKEKLVELDD CPEDLYLIEG DVDAFDDSSF NAEELEGAVC VQLNQRQMRY SRFPAIPLFG
RAAREQRLEL LREERDEVVE QHAKASFDSQ KLQRLYASFN QFVAMHLQVA FDADPEQALA
NARDKRNQLL RSISEFEAQE QQLRSQLQAS KQALAALDKL APQMGLLDED 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
//
