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Database: UniProt
Entry: A4YPN2_BRASO
LinkDB: A4YPN2_BRASO
Original site: A4YPN2_BRASO 
ID   A4YPN2_BRASO            Unreviewed;      1154 AA.
AC   A4YPN2;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   OrderedLocusNames=BRADO2000 {ECO:0000313|EMBL:CAL75858.1};
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL75858.1, ECO:0000313|Proteomes:UP000001994};
RN   [1] {ECO:0000313|EMBL:CAL75858.1, ECO:0000313|Proteomes:UP000001994}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
CC   -!- FUNCTION: Required for chromosome condensation and partitioning.
CC       {ECO:0000256|HAMAP-Rule:MF_01894}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC   -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC       each terminus and a third globular domain forming a flexible hinge near
CC       the middle of the molecule. These domains are separated by coiled-coil
CC       structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC   -!- SIMILARITY: Belongs to the SMC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01894}.
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DR   EMBL; CU234118; CAL75858.1; -; Genomic_DNA.
DR   RefSeq; WP_011925080.1; NC_009445.1.
DR   AlphaFoldDB; A4YPN2; -.
DR   STRING; 114615.BRADO2000; -.
DR   KEGG; bra:BRADO2000; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_3_5; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000001994; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   CDD; cd03278; ABC_SMC_barmotin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01894; Smc_prok; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   InterPro; IPR011890; SMC_prok.
DR   NCBIfam; TIGR02168; SMC_prok_B; 1.
DR   PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   Rule:MF_01894};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001994}.
FT   DOMAIN          3..1135
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   DOMAIN          507..545
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|Pfam:PF06470"
FT   REGION          454..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..197
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          644..713
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          748..990
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1154 AA;  127270 MW;  A5F32481783F963E CRC64;
     MKLTRLRLHG FKTFVEPTDF VIEPGLTGVV GPNGCGKSNL VEALRWAMGE TSHKSLRAAD
     MDAVIFSGSN TRPSRNHAEV VMTIDNSDRT APAAVNDRDI LEISRRIERE AGSVYRINGR
     DVRARDVQIL FADAATGARS PALVHQGKIG EIIQAKPEQR RRVLEDAAGV AGLHARRHEA
     ELRLKAAETN LLRVEDVIGQ LSGQMEGLRK QARQAIRYRE VAAKVRKAEA TLYHLRWMGA
     HADLNDAAHT HDVAVREMAE RTREQAESAR IQAIRSSHLP ALREAEARAA ATMQRLKNAR
     DLLDREEVRA KERAGELDRR LMQLTADVAR EQQQNQDAQV ALQRLETEDA ELKEEIKARV
     EMRSGVDERV AEAEALLLET ERQFTELTTQ LADLTARRNQ LEANVRSHRE RLARLDQDIA
     NVRADEERLA QETAHLGDLD TLAAALEAAE EAEAQAEAAV QTNEAAQANA RQKLEASRAP
     LADAEKRAQR LETEARTISK MVNSETKNLW PPIIDGVTVA KGYEKALGAV LGDDLDAPVD
     ASAPMHWTVA GAEVTDPALP DGVEPLAAYV QAPPELSRRL AQIGVVSRER GAQLVSQLRT
     GQRLVSPEGD VWRWDGFIAA AHAPTGAARR LAERARLIDI EAELEQARID AAGKRQALES
     AEAEVKAATA AESAAREAWR AAQREVNSAR ERHANAEREI NRHSARKSAL VEASTRLAHD
     RAEIAELHQN ALEAIEELPA TTEADGRLAA VRAEIETKRR AAAQVRAEAQ ALAREAELAD
     RRVQAIINER NDWFNRIRGA GSQIATIEAR IAEVRDERAE LDNAPEIFAE KRSALIDELA
     IAEEERQVAA DALAEAETAM GDTDRAAKAS LEALSKSREA AARAEERLES AKRRVADVER
     EIHDMLECEP NAVAAMAEIG PDTQLPPLHE IEDSLEKLRR DRERLGAVNL RAEEELTEVE
     GSHTALTTER DDLVEAIKRL RQGIQSLNKE ARERLQASFE TVNDHFKRLF TELFGGGEAA
     LHLIESDDPL EAGLEIIAKP PGKKPQTLSL LSGGEQALTA MALIFAVFLT NPSPICVLDE
     VDAPLDDHNV ERFCNLLHEM KGSTETRFII ITHNPITMAR MNRLFGVTMA ERGVSQLVSV
     ALDEAVKILD QQVA
//
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