ID A0A0F2P8F0_9GAMM Unreviewed; 1168 AA.
AC A0A0F2P8F0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=VR73_01340 {ECO:0000313|EMBL:KJS09715.1};
OS Gammaproteobacteria bacterium BRH_c0.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS09715.1, ECO:0000313|Proteomes:UP000033581};
RN [1] {ECO:0000313|EMBL:KJS09715.1, ECO:0000313|Proteomes:UP000033581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS09715.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS09715.1}.
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DR EMBL; LADM01000012; KJS09715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2P8F0; -.
DR STRING; 1629722.VR73_01340; -.
DR PATRIC; fig|1629722.3.peg.3138; -.
DR Proteomes; UP000033581; 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; 2.
DR Gene3D; 1.20.1060.20; -; 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 521..621
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 776..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..238
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 300..341
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 370..432
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 872..913
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 1168 AA; 131897 MW; 208FF9B27A0E60F0 CRC64;
MRLKSIKLAG FKSFVDPTTV HFPSNLCAVV GPNGCGKSNV IDAVRWVMGE SSAKHLRGES
MTDVIFNGSG GRKPVGQASI ELIFDNSDGT LGGEYASYAE ISIRRKVTRD GQSGYYLNGN
KCRRRDITDI FLGTGLGPRS YAIIEQGMIS NLIEARPEDL RVFIEEAAGI SKYKERRRDT
ENRMRRTHEN LERLTDIRDE LGRQLQRLER QAQAAEKYAE FKKEERQAKA QLQALRWREF
NAQVQSRQVL ISRQELDVEA LVTERSSCDN ALEKLRVQYT DQSDGFNAVQ GEFYAIGAEV
ARTEQSIEHV RQRARELRQD IEQTERNYAE SEQHLRSDRA RAEGWEAELA EISPTLETLG
AEEEESSILL QAAEEAMNQW QSAWDEFNQR AAQPRQQAEV QQSRIQHLEQ VLRRLGERIE
RLDSERRELI STGPGEEDLA LLDEQLAEME MTGGDMQSQL ETMVSSIDET RKSYQAAGQE
LGQVREQIQS LKGRQSSLEA LQQAALEDNG EEKQWLDQQG LTGAARLAES LEVQPGWEVA
LETVLGSGLQ AVCVDVLDPL ISALDSLGKG ELTLLDSTPS APVPAEAGRV SLASLVQGNQ
ATSLLAGIHS AENLDAALAL RSGLAAGESV VTREGVWLGP NWVRVARGKN AAAGVLKRKQ
ELAELHSQLE SLSVRSEQLA ALQMTREQEL SSLERQRETL SRTIAERQRE YAELRSRVSA
SRMQIEQFAA RRNRAEDELA EIRQQQQLEQ EGLGEARVIL QDALDAMETD TRQRETLLTE
RDQARNSLDS ARQRARHTRD RLHELSMRER SVSTQLQAVK EGLGRLEIQV ARLQERRDQL
LASVNLEEDP TEELTLQLEE QLEKRLLVER RLAQARVSLE EVEHGMREHE KRRSQLENLI
LDKRTELEQT RLQTQEVRTR CNTIAEQIAE QGYQLQSLLD ELGEEADPRQ WEEELERIAA
RIQRLGAINL AAIEEFKTES ERKTYLDAQH NELTEALETL EGAIRKIDRE TRTRFRETFE
KINQSLEELF PKVFGGGHAY LELTGDDLLD TGVTIMAQPP GKKNTTIHLL SGGEKALTAI
ALVFSIFRLN PAPFCMLDEV DAPLDDANVG RYARMVQEMS DRVQFIYITH NKIAMEMAQH
LMGVTMHEPG VSRLVSVDVD KAVELAEA
//
