ID F2I6B2_AERUA Unreviewed; 1186 AA.
AC F2I6B2; A0A9Q4H235;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:AEA00897.1};
GN OrderedLocusNames=HMPREF9243_1548 {ECO:0000313|EMBL:AEA00897.1};
OS Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC Aerococcus incertae sedis.
OX NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA00897.1, ECO:0000313|Proteomes:UP000008129};
RN [1] {ECO:0000313|Proteomes:UP000008129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL Submitted (FEB-2011) 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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; CP002512; AEA00897.1; -; Genomic_DNA.
DR RefSeq; WP_013669142.1; NZ_JAOTMI010000005.1.
DR AlphaFoldDB; F2I6B2; -.
DR STRING; 866775.HMPREF9243_1548; -.
DR KEGG; aur:HMPREF9243_1548; -.
DR PATRIC; fig|866775.3.peg.1453; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000008129; 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 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: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; 2.
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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000008129}.
FT DOMAIN 518..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 702..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..496
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 826..944
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 702..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1186 AA; 134379 MW; BCDB399F0F42C304 CRC64;
MYLKTIEMVG FKSFAEKTRV ELDQGFTAIV GPNGSGKSNI TEAVKWVLGE QSAKSLRGKR
MDDVIFSGSQ SRRQSQYAQV VLTFDNRDRV LDMDSDEVSV LRRYTRSGDS IYKINGQNCR
LKDITQLMMD TGVGKESFSI ISQGKVEEIF TQRAEERRAI FEEAAGVMKY KSKKQEAERK
LDRSQENLNR IEDILSEIEG RLEPLKEQKE AAVSYRDKKQ ELSQIEIALT AVQIETLNEQ
WQLAKQDLES IQASNEAKKR QLDKEETALA QAKVAEEQSD DRVNDLNDNY VVKLQAVEKL
RSQLQMMEQE QRFIQSNRQS QEKEQANLQA KIEKMKTDLK SNQAQLDKYQ KTYQSQADSY
QSLKDQLAAL SDYSQEDLED LRNQYIAYLQ EESHLSNQIQ QTEKDIQQGQ KNQEKYAERI
RISQKEQAKL EDQQEGLDQE ISQKEQALKN LLQEYQIQAQ SLQQAQDQVQ KATNANQTLY
QKLLRKQAQL DSLKNLEDNH EGFYYGVKNA LKLKSQKRGI FGAIAELIDV PEDYTLAVET
ALGGSMQNIV TQDGQVAQEV IAYLKAKKAG RATFLPLDTM KSRRISDQQV SHVQADPAYI
GLLVDLVDFD DQFQTVMENV MGNIILAEDL TGARRLSQAL HARYRVVTLT GDLVNAGGSL
TGGANKRNQT SLLSRKNDIQ SLSQAIESME VAYQEAASRI ATQQQGQDQM SQALESLKEK
GSESRYDLRS SQTEREHLTQ ELEKLAKEVQ GQDYEKNLSQ EDVKQSQADL ATSQEKLTHL
QEKIQAAKAK IDARLLSDEE KGQQKARLQE DFQQIATDFA VTKEQFKQAK DQKASLSAEL
ADQEKAYQEL SNLLSQALTN DSDQEEKKKH LEAQLQSFQK QSKDIQTQLK TAKEERQEAS
QKVEAANQMI SQLNLEIQSN LQSIAKLEAS VSRYEVSIDN HLEQLSESYG LTYERARAES
QLTMSIDQAS SRVKQLKQAI DSLGPVNMQA IEEYDEVYER FCFIDKQRQD AIDARENLYQ
TIAEMDSEVS TRFKTTFEAI RDAFESIFPA LFGGGKATLK LTDPNDLLNT GVEIMAQPPG
KKLQLLSLLS GGERALTAIA LLFAILDVKT VPFSILDEVE AALDDANVAR YGRYLQKFAQ
KTQFIVISHR KGTMEAANIL YGVTMQQEGI SQLASVRLED VDDQLN
//
