ID A0A0M0HT94_VIBNE Unreviewed; 1485 AA.
AC A0A0M0HT94;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:KOO05289.1};
GN ORFNames=AKJ17_00360 {ECO:0000313|EMBL:KOO05289.1};
OS Vibrio nereis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=693 {ECO:0000313|EMBL:KOO05289.1, ECO:0000313|Proteomes:UP000037515};
RN [1] {ECO:0000313|Proteomes:UP000037515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19584 {ECO:0000313|Proteomes:UP000037515};
RA Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT isolated from the Solomon Islands.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KOO05289.1}.
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DR EMBL; LHPJ01000001; KOO05289.1; -; Genomic_DNA.
DR RefSeq; WP_053393800.1; NZ_LHPJ01000001.1.
DR STRING; 693.AKJ17_00360; -.
DR PATRIC; fig|693.5.peg.73; -.
DR OrthoDB; 6722439at2; -.
DR Proteomes; UP000037515; 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; -; 2.
DR Gene3D; 3.40.1140.10; -; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000037515}.
FT DOMAIN 2..227
FT /note="MukB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04310"
FT DOMAIN 647..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 COILED 302..433
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 560..590
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 640..667
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 889..1028
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 1055..1110
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 1485 AA; 169079 MW; 88B1E093A316E701 CRC64;
MIERGKYQSL TMVNWNGFFA RTFDIDGLVT TLSGGNGAGK STTMAAFITA LIPDQTLLHF
RNTTEAGSSQ SSRDKGLYGK LQPGACYAAL DVVNSRNQRL LFAVKLQQVA GRDKKVDIKP
FVIQGLPSHV KPTDVLVESV SATQARVRQI NEVKDAIAEF EGVQFKSFSS IVEYHAQMFE
FGVVPKKLRN SSDRSKFYRL IEASLYGGIS SAITRSLRDY LLPQNGGVKK AFQDMESALR
ENRMTLEAIK TTQADRDLFK HLITESTNYV AADYMRHAND RRNKLDKTLA LRSELFGSRE
TLVEQNNLLN RVQEELELLV ESESALEQDY QAASDHLQLV QNALRQQEKI SRYQEDLEEL
SERLEEQVMV VEEAQERVLM AEEQATVSEE EVDSLKTQLA DYQQALDVQQ TRALQYQQAV
QALEKAKQLL DDESLTAESA QTLVSDLKTQ ESENTNTLLS VKHKLDMSSA AAQQFDTALK
LVQSIVGQVE RKEAAGHAKQ VLQKARNAEH VAQNEQQWRA QHRDLERSLN QQRQARELVD
GYRKQHHVEL TDEIAFEQER ERHAMQIESL EMAQEDIREE RSEQRRIEQD SASEIRKLEA
IAPTWIAAND ALETLREQSG AELHDSQAVM SQMQVVLEQE KQQSLAKDKL AERRAQLENE
IERLASPGGS NDSRLKGLAD TLGGVLLSEI YDDITIDDAP YFSAMYGPAR HAIVVSDLSG
IEEKLVELDD CPEDLYIIEG DVDAFDDSSF NAEELEGAVC VRMNERQMRY SRLPEIPLFG
RAAREQRLEL LRVERDEVVE QHAKAAFDSQ KLQRLYQAFN SFVAKHIQVA FESDPEQALA
GLREKRNHVV RLLADLDAKE QQQRSQLQSS KQALSALDKL APHMALIEDE TLQARFDELE
EKITQLSEAK AFLNSHGKAL AELEKVATAL EADPEQFDAL EAEYKAADQR LQDLKKQIFA
LSDLVERRHY FAYSDSVDLL NKSSELSEQL KSKLVQAERA RTRAREELKQ SQGQINQYNQ
VLASLKSSHQ AKLETVQEFK QELQEFGVNA DEGAEERAMR RRDELQERLH TSRSRKSEYE
RTITSTELEM KGLAKRLKKV QKEYAELRKF VVAAKAGWCS VLRLARENDV ERRLHKRELA
YMSADELRSM SDKSLGALRL AVADNDDLRD ALRLSEDNAR PERKVLFYIA VYQHLRERIR
QDIIHTDDPV EAIEEMEVEL ARLTEELTQR ENRLAISSES AASIIKKTIQ REQNRIRMLN
QGLSNIGFGQ VKGVRLNVKI RESHEILLHG LASQQEQHKD LFETSRYTFS EAMAKLFQRV
NPHIDMGQRS PQVLGEELLD YRNYLELSVE VNRGSDGWLQ AESGALSTGE AIGTGQSILL
MVVQSWEEES RRLRSKDIVP CRLLFLDEAA RLDAKSISTL FELCDRLDMQ LLIAAPENIS
PEKGTTYKLV RKVFKDHEHV HVVGLRGFGQ TEKPKSEAQE LIEEL
//
