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Database: UniProt
Entry: A0A494XXM9_9BURK
LinkDB: A0A494XXM9_9BURK
Original site: A0A494XXM9_9BURK 
ID   A0A494XXM9_9BURK        Unreviewed;      1172 AA.
AC   A0A494XXM9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN   ECO:0000313|EMBL:RKP52869.1};
GN   ORFNames=D7S89_04285 {ECO:0000313|EMBL:RKP52869.1};
OS   Trinickia fusca.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Trinickia.
OX   NCBI_TaxID=2419777 {ECO:0000313|EMBL:RKP52869.1, ECO:0000313|Proteomes:UP000280434};
RN   [1] {ECO:0000313|EMBL:RKP52869.1, ECO:0000313|Proteomes:UP000280434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7MK8-2 {ECO:0000313|EMBL:RKP52869.1,
RC   ECO:0000313|Proteomes:UP000280434};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Paraburkholderia sp. 7MK8-2, isolated from soil.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
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:RKP52869.1}.
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DR   EMBL; RBZV01000001; RKP52869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494XXM9; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000280434; Unassembled WGS sequence.
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; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 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; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
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:UP000280434}.
FT   DOMAIN          518..625
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          170..211
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          251..369
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          405..506
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          666..894
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          992..1019
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   1172 AA;  130170 MW;  09B553E9819980EE CRC64;
     MRLTSIKLAG FKSFVDPTHF QVPGQLVGVV GPNGCGKSNI IDAVRWVLGE SRASELRGES
     MQDVIFNGST ARKPGSRASV ELVFDNADGR AAGQWGQYTE IAVKRVLTRD GTSSYYINNL
     PARRRDIQDI FLGTGLGPRA YAIIGQGMIA RLIEAKPEEL RVFLEEAAGV SKYKERRRET
     ENRLHDTREN LTRVEDIVRE LGTNLEKLEA QAVVATKFKT LQAEGEEKQR LLWLLRKNDS
     AAEQGRQQRA ISDAQIDLEA QTARLREVEA ELETLRVAHY AASDAMQGAQ GALYEANAEV
     SRLEAEIKFI IESRNRTQAQ IAALTAQREQ WQMQAEKARG DLEDAEEQLA MAEEKAAQAE
     DEAAAKHDAL PALETRWRDA QTQLNDERGG IAQTEQSLKL EAAHQRNADQ QLQQLQQRHE
     RLKAEAGGLD APDEVQLEEQ RMQLAEHEEI LREAQQRLAE AQEALPQLDA ARREAQQRVQ
     SESAQIHQFE ARLVALKQLQ ENVQTEGKIQ PWLDKHELAG LSRLWKKLHV EAGWETALES
     ILRERLAALE ISNLDWVKAF ASDAPPAKLA FYSPPAAGAP RETPAGLRPL ISLVRIDDAG
     LRAVLSDWLG HVYLADDLTQ ALAMRAQLPE GGALVVKAGH VVTRVGVQLY AADSEQAGML
     ARQQEIENLT RQLRAQTLLA DEAKTASIRA EAAHTQASQA LADVRAQAER ATQRVHALQM
     DVLKLTQAHE RYTQRSTQIR EELEEIAAQI DEQRAQRAES EANFERHDGE LAELQARFEE
     HQLAFEALDE ALGEARTQAR DLERGATDAR FAARNMANRI DELKRTIQVA HDQSERVAAS
     LEDARAELET INEQTTHTGL QDALEIRTAK ESALSAARIE LDDLTAKLRH MDETRLTVER
     SLQPLRERIT ELQLKEQAAR IAGEQFIEQL AAANVDEAQL QEKLTPDMKP SYLQGEVTRI
     NNAITALGPV NMAALEELAA ATERKTFLDA QSADLTSAIE TLEDAIRKID QETRTLLQAT
     FDEVNRHFGE LFPRLFGGGQ AKLIMTGDEI LDAGVQVMAQ PPGKKNSTIH LLSGGEKALT
     ATALVFAMFQ LNPAPFCLLD EVDAPLDDAN TERFANLVRA MSDKTQFLFI SHNKIAMEMA
     QQLIGVTMQE QGVSRIVAVD METAAGFAQN TA
//
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