ID   A0A379C8D8_9PAST        Unreviewed;      1497 AA.
AC   A0A379C8D8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Structural maintenance of chromosome-related protein {ECO:0000313|EMBL:SUB58570.1};
GN   Name=mukB {ECO:0000313|EMBL:SUB58570.1};
GN   ORFNames=NCTC12872_00534 {ECO:0000313|EMBL:SUB58570.1};
OS   Phocoenobacter uteri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Phocoenobacter.
OX   NCBI_TaxID=146806 {ECO:0000313|EMBL:SUB58570.1, ECO:0000313|Proteomes:UP000255417};
RN   [1] {ECO:0000313|EMBL:SUB58570.1, ECO:0000313|Proteomes:UP000255417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12872 {ECO:0000313|EMBL:SUB58570.1,
RC   ECO:0000313|Proteomes:UP000255417};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UGTA01000001; SUB58570.1; -; Genomic_DNA.
DR   OrthoDB; 6722439at2; -.
DR   Proteomes; UP000255417; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0009295; C:nucleoid; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
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   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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255417}.
FT   DOMAIN          35..259
FT                   /note="MukB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04310"
FT   DOMAIN          678..843
FT                   /note="MukB hinge"
FT                   /evidence="ECO:0000259|Pfam:PF16330"
FT   REGION          1082..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          375..496
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          540..633
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          871..941
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1016..1050
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1082..1099
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1497 AA;  172182 MW;  3618DD32892B0243 CRC64;
     MTEQQFELEQ EQQELQKTAE ITPLTSTVVT KKESIARGKF VSLTLINWNG FFARTFDLDD
     LVTTLSGGNG AGKSTTMAGF VTALIPDLTL LNFRNTTEAG STAGSRDKGL HGKLKSGVCY
     AVLESENSRK QRIISGVRLQ QVAGRDKKVD IRPFSLQNLP LEQSIISILT EKVADRSARV
     LALNELKEKC ESTEIQFKQY NSITDYHSFL FDLGVLPKRL RSASDRSKFY KLIEASLYGG
     ISGAITKSLR EYLLPENTGV RQAFQDMESA LRENRMTLEA IKVTQSDRDM FKKLITESTN
     YVSADYMRNA NERRGNVENV LAQRKNWQEV KAKIELSQTQ LVEYSREVSE IAETESHLET
     EFNSATDHLN LVMNALRHQE KVERYQDEVN DLVEKIEEQQ MAMEELSEQV ESSQFRAEEA
     EEVVEDLRSQ LADYQQALDA QQTRALQYQQ AVQALEKAKQ VCGLPNLDLH NIQDYAVEFE
     AQAEELTDKV FELEQRLSVS EIAKEQFDKA YDLVCKISGK IDRSEAWSEA KALLSAYPSQ
     KSQANQAVSL RQKLNELERK LQQQQNAERL LNEFNHKAQT DFTTAEELES YFEEQQASLE
     DIEAELGEVV EVRSTQRQQL EQLNQQYQKL TQIAPAWHTA QSALARLQEQ CDREFEASQQ
     VMAFMQDTLN SEREITLERD KLARKSDRLE EQITRLSQPD GSEDPRLNQL AERFGGVLLS
     ELYEDVSIDD APYFSALYGE ARHAIVVRDL ESVKSQLEQL DDCPDDLYLI EGDPSSFDDD
     VFEATELGDG VVVQVSNRQW RYSKFPQVPL FGRAAREKQL ELLKAEQEDI TEQHAKFAFK
     VQKCQRLYQH LSQFVGTHLS LAFEVNPEQA MQEISAQRVE IERELNQISG NEQQLRHKRD
     NCKEQLQLLN KALPQVELLA DETLIDRAEE CKEQLLEAQE DEQFIRQFGQ YLAQLEPIAT
     ALQSDPTKFE QLEDEYKRSV FDQKLRKQQV FCLSDVMNRR LHFSYEDSTQ EGSELTEQLR
     VRLENAQRER EQAKAQFRQA QTQYTQYNQV LTSLRSSYEA KNEMLVELVR EIDELGLRGD
     SEAEERARMQ RDELQQRLSQ QRSRKSYLEK QLAVIEADMD NLNRAICKAE RDYKVLREQV
     VQAKVSWCVV MRLSRNSDVE KRLNRRELAY MSSEELRSIS DKALGALRIA VADNEYLRDS
     LRASEDNRKP ENKVAFFIAV YQHLRERIRQ DIIKTDDPID AIEQMEIELS RLTSELTNRE
     KKLAISSESV ANILRKTIQR EQNRILQLNQ GLQNITFGQV KGVRLVVNIR DTHAILLNAL
     STEKENHKDL FESDTLGFSE ALAMLYKRVN PHLELGQRTA QTIGEELLDY RNYLDLDVET
     YRGADGWMKA QSSSLSTGEA IGTGMSILLM VVQSWEEESR RMRAKDILPC RLLFLDEAAR
     LDAKSINTLF ELCDRLDMQL LIAAPENISP EQGTTYKLVR KIANNQEYVH VVGLKGF
//