ID A0A2S7JMQ7_9BURK Unreviewed; 1171 AA.
AC A0A2S7JMQ7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:PQA81534.1};
GN ORFNames=C5F52_20315 {ECO:0000313|EMBL:PQA81534.1};
OS Limnohabitans sp. TS-CS-82.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=2094193 {ECO:0000313|EMBL:PQA81534.1, ECO:0000313|Proteomes:UP000238850};
RN [1] {ECO:0000313|EMBL:PQA81534.1, ECO:0000313|Proteomes:UP000238850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TS-CS-82 {ECO:0000313|EMBL:PQA81534.1,
RC ECO:0000313|Proteomes:UP000238850};
RA Shabarova T., Salcher M.;
RT "Limnohabitans TS-CS-82.";
RL Submitted (FEB-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:PQA81534.1}.
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DR EMBL; PTQX01000011; PQA81534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7JMQ7; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000238850; 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; 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}.
FT DOMAIN 518..624
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 791..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 335..478
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 880..907
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 988..1015
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 1171 AA; 129697 MW; 7C3675024AD7C8E9 CRC64;
MRLNSIKLSG FKSFAEPTNF LLPGQLVGVV GPNGCGKSNI MDAVRWVLGE SKASELRGES
MQDVIFNGTT TRKPASRSSV ELVFDNADHR AGGQWSQFPE IAVKRVLTRD GGSSYFINNQ
PVRRRDVQDV FLGTGLGPRA YAIIGQGTIS RIIESRPEEL RLFLEEAAGV SKYKERRRET
ENRLSDTREN LTRVEDILRE LNANLEKLEK QAEVAQRYHA LQGDVTLKQH QLWFLRRAEA
EADQLGLKTQ ADKAVNDLES RIADLRHIEA DLETVRQAHY AAGDQVNQAQ GALYEASAEV
GRLEAEIRFV VEGRQRAEAR LVQIKEQTAH WAQQSEQASE EIENLASAAM DGEERAVMLA
AQVEEQAMQL PDLEEAVRTA QQRSNEQRAS VAQVQQQIQV LAADQRNIEE QSRQLNSRHE
RLSADRNALA SPDEVRLTHL QEQLQDAQAT AEITAAQLEE LQANVPQLDE ARRTAQQTVN
TEQAKQADIS ARLEALKALQ EKVQTDDKLK PWLTKHGLDG LQALWSRIHI DAGWENALEA
ALRERMASLE VSRLDIVRAF QADAPPAKLA FYTPPMAGVA APQGALPRLS DLLRLNDAGL
QGLLTDWLSG CFTAPNLDEA LAKRASLQPG HVIYVPSGHA ISAHSVTFYA QDSAQSGLLA
RAQEIENLDK STKAQAFISD EARHNLVRAE ATYSESSQRL VSIRAEATAA QARAHELQVE
TLRLTQLAEQ TRARSAQLSG DLAEVEAQLA DLQERRVNAE GRFEELDMQL ADSQERHAQL
DDAVINAERR LNDSREQQRS LERQAQEAQF SQRSLATREA ELKRIIDTAT QQAASVAAEE
ARVQEDLTRL TDAAAQAGLQ NALNTKMERE VALGAKRSEY DDLTTKLRAS DERRLQLERE
LEPLRQRITD FQLKEQAARL GLEQYSQLLA DAQADLEAVG ASIQANNVRL GGLQSEIDRL
NRDITALGAV NLAALDELAI ASERKVFLDS QTKDLTDAMN TLEDAIRKID GETRELLGGT
FKIVNEHFGR MFPELFGGGN ARLVMTGDEI LDAGVQVLAQ PPGKKNQTIH LLSGGEKALT
AIALVFAIFQ LNPAPFCLLD EVDAPLDDAN TERYAKLVSS MSKETQFLFI SHNKIAMEMA
EQLIGVTMQE QGVSRIVAVD MESAVSMVES V
//
