GenomeNet

Database: UniProt
Entry: A0A1N6MZJ7_9GAMM
LinkDB: A0A1N6MZJ7_9GAMM
Original site: A0A1N6MZJ7_9GAMM 
ID   A0A1N6MZJ7_9GAMM        Unreviewed;      1485 AA.
AC   A0A1N6MZJ7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:SIP74255.1};
GN   ORFNames=XIS1_600021 {ECO:0000313|EMBL:SIP74255.1};
OS   Xenorhabdus innexi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=290109 {ECO:0000313|EMBL:SIP74255.1, ECO:0000313|Proteomes:UP000196435};
RN   [1] {ECO:0000313|Proteomes:UP000196435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGB1681 (deposited as PTA-6826 in the American Type Culture
RC   Collection) {ECO:0000313|Proteomes:UP000196435};
RA   Gaudriault S.;
RL   Submitted (DEC-2016) 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   ---------------------------------------------------------------------------
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; FTLG01000204; SIP74255.1; -; Genomic_DNA.
DR   OrthoDB; 6722439at2; -.
DR   Proteomes; UP000196435; 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; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01800}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_01800};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_01800};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW   Rule:MF_01800}; Coiled coil {ECO:0000256|HAMAP-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:UP000196435}.
FT   DOMAIN          2..227
FT                   /note="MukB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04310"
FT   DOMAIN          645..810
FT                   /note="MukB hinge"
FT                   /evidence="ECO:0000259|Pfam:PF16330"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT   REGION          993..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          343..464
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT   COILED          515..600
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01800"
FT   COILED          838..865
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;  170824 MW;  FFAB4AA624CA976B CRC64;
     MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LRAGVCYSTL DVVNSRHQRV IAGVRLQQIA GRDRKVDIKP
     FMIQGVPASI QPTQLLTENI NERQARVLPL NELKERLEEM DGVQFKQFNS ITDYHSLMFD
     LGVIPKRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRVTLEAIR VTQSDRDLFK HLITEATAYV SADYMRHANE RRVHLDEALA LRSELFGSRR
     QLVTEQYRHV EMARELTEQS GASSDLEMDY QAASDHLNLV QTAMRQQEKI DRYQADIEEL
     TYRLEEQTEV VEEAKEMQAE YEAASEAAEQ EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
     QALERARELC QLPELSAENA DEWQETYQAK EQQATETLLA LEQKLSVADA AHSQFEQAYQ
     LVKNIVGEVS RSEAWHRARE VLREWSSQRH LAERVQPLRI QLAELEQRLN SQQNAERMLE
     EFCKRHHQQY QAEDLEVLQG ELEAQLEELS LTANESGESR MQVRQELEQL RQKIQTLTAR
     APVWLAAQET LDQLCEQSGE TFEDSNDVTE YMQQLLEQER ETTVERDNVS AQKRELEKQI
     ERLSQPSGAE DSRLLALAER FGGVLLSEIY DDITIDDAPY FSALYGSARH AIVVPDLSLV
     RPHLEALEDC PEDLYLIEGD PQSFDDSVFD FEEQENAVLV KSSDRQWRYS RYPEVPLFGR
     AARENRLEAL GLERDTLAER YATLSFDVQK IQRAHQAFSR FVGKHLSVAF DSDPEMEIRS
     LNQRRTELER ELSQFESHTQ QNQQKLTQVK ESLSVLNRLI PQIAILLDET LIDRVEAVRE
     EMSEAQDAAR FLQQHTNTLN KLEPMVSVLQ SDPRQHEQLQ RDYELVKQSQ IKAKQQAFAL
     TEVVQRRVHF SYSDSAGMLS ENSDLNDKLR QRLEHAESDR SRAREQLRQQ QSQSAQFSQV
     LASLKSSYDT KQDMLKELEQ EMKDIGVQAD ANAENRARER RDQLYASVQA NRSRINQLEK
     QIAFCEAEME NLQKKLRKSE RDYYQKREQV VSSKAGWCAV MRMVKDNGVE RRLHRRELAY
     MDADALRSMS DKALGALRLA VADNEHLRDA LRLSEDPKRP ERKIQFFVAV YQHLRERIRQ
     DIIRTDDPVD AIEQMEIELA RLTEELTARE QKLAISSKSV ANIIRKTIQR EQNRIRMLNQ
     GLQMVSFGQV GGVRLNVNIR ESHAALLDVL SEQQEQHQDL FNSQRLTFSE AIAKLYQRLN
     PQIDMGQRLP QTIGEELLDY RNYLELDVEV NRGSDGWLKA ESGALSTGEA IGTGMSILVM
     VVQSWEEESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCERLQMQL IIAAPENISP
     EKGTTYKLVR KIFNNQEHVH VVGLRGFGQE TPVIEQRQEQ AQAIF
//
DBGET integrated database retrieval system