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
//