ID A4NYF6_HAEIF Unreviewed; 1510 AA.
AC A4NYF6;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 ORFNames=CGSHiR3021_04837 {ECO:0000313|EMBL:EDK13802.1};
OS Haemophilus influenzae 22.4-21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=375063 {ECO:0000313|EMBL:EDK13802.1, ECO:0000313|Proteomes:UP000005596};
RN [1] {ECO:0000313|EMBL:EDK13802.1, ECO:0000313|Proteomes:UP000005596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22.4-21 {ECO:0000313|EMBL:EDK13802.1,
RC ECO:0000313|Proteomes:UP000005596};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAZJ01000006; EDK13802.1; -; Genomic_DNA.
DR Proteomes; UP000005596; 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 43..267
FT /note="MukB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04310"
FT DOMAIN 686..851
FT /note="MukB hinge"
FT /evidence="ECO:0000259|Pfam:PF16330"
FT REGION 707..824
FT /note="Flexible hinge"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 349..504
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 673..700
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 879..949
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 977..1052
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT COILED 1121..1148
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT BINDING 75..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1510 AA; 173298 MW; 11D6B6D0A5940DCC CRC64;
MSDVFELENE IELESDEVIM ENENVEEIVD ASIPFSMTTN NGVERGKFRS LTLINWNGFF
ARTFDLDELV TTLSGGNGAG KSTTMAGFVT ALIPDLTLLH FRNTTEAGST GGSRDKGLHG
KLRPGVCYAV LDTINSRHQR ILVGVRLQQI AGRDKKVDLK TFSIQGVELS QNPTALFTET
VGERQARVLN LNELKDKIEN IGAQFKQYHS ITDYHGMMFD LGIIPKRLRS ASDRSKFYKL
IEASLYGGIS SAITRSLRDY LLPENLGVRK AFQDMESALR ENRMTLEAIK VTQSDRDLFK
HLITETTNYV ASDYMRNANE RRGNIETALE SRREWYKAKA EQNLSQHRLI DLSREAAELA
ENERTLEVDH QSAVDHLNLV LNALRHQEKI TRYQEDIAEL TERLEEQKMV VEDANDALEE
SQAQFEQTEI EIDAVRSQLA DYQQALDAQQ TRALQYQQAI AALEKAKTLC GLADLSVKNV
EDYHAEFEAH AESLTETVLE LEHKMSISEA AKSQFDKAYQ LVCKIAGEMP RSAAWESAKE
LLREYPSQKL QAQQTPQLRT KLHELEQRYA QQQSAVKLLN DFNQRTNLSL QTAEELEDYH
AEQEALIEDI SAGLSEQVEN RSTLRQKREN LTALYDENAR KAPAWLTAQA ALERLEQQSG
ETFEHSQDVM NFMQSQLVKE RELTMQRDQL EQKRLQLDEQ ISRLSQPDGS EDPRLNMLAE
RFGGVLLSEL YDDVTIEDAP YFSALYGPAR HAIVVRDLNA VREQLAQLED CPDDLYLIEG
DPTAFDDSVL SAQELELGVV VQVSDRELRY SRFPEIPLFG RAAREKRLEE LQIERDEVAE
QHAQIAFDVQ KCQRLYEHFS QFVGLHLALA FQPNPEELMS EINRERNEID RELNQFNNGE
QQLRIQLDNA KEKLQLLNKL IPQLNVLADE DLIDRIEECR EQLDIAEQDE YFIRQYGVTL
SQLEPIANSL QSDPENYEGL KNELTQAIER QKQVQQRVFA LADVVQRKPH FGYEDAGQAE
TSELNEKLRQ RLEQMQAQRD TQREQVRQKQ SQFAEYNRVL IQLQSSYDSK YQLLNELIGE
ISDLGVRADD GAEERARIRR DELHQQLSTS RQRRSYVEKQ LTLIESEADN LNRLIRKTER
DYKTQRELVV AAKVSWCVVL RLSRNSDMEK RLNRRELAYL SADELRSMSD KALGALRTAV
ADNEYLRDSL RVSEDSRKPE NKVRFFIAVY QHLRERIRQD IIKTDDPIDA IEQMEIELSR
LTAELTGREK KLAISSESVA NIMRKTIQRE QNRIRMLNQG LQNIAFGQVK SVRLVVNIRD
THAMLLDALS GQQNEYQDLF NDNRITFSEA MAKLYQRINP HIDMGQRTAQ TIGEELLDYR
NYLELEVEVF RGADGWLRAE SGALSTGEAI GTGMSILLMV VQSWEEESRR IRGKDIVPCR
LLFLDEAARL DGKSISTLFE LCERLDMQLL IAAPENISPE KGTTYKLVRK IAGNQEHVHV
VGLRGFGATD
//
