ID A0A0S2TEG6_9GAMM Unreviewed; 1169 AA.
AC A0A0S2TEG6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=Tel_10240 {ECO:0000313|EMBL:ALP53492.1};
OS Candidatus Tenderia electrophaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Tenderia.
OX NCBI_TaxID=1748243 {ECO:0000313|EMBL:ALP53492.1, ECO:0000313|Proteomes:UP000055136};
RN [1] {ECO:0000313|EMBL:ALP53492.1, ECO:0000313|Proteomes:UP000055136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRL1 {ECO:0000313|EMBL:ALP53492.1};
RA Eddie B.J., Malanoski A.P., Wang Z., Hall R.J., Oh S.D., Heiner C., Lin B.,
RA Strycharz-Glaven S.M.;
RT "Description of Candidatus Tenderia electrophaga gen. nov, sp. nov., an
RT Uncultivated Electroautotroph from a Biocathode Enrichment.";
RL Submitted (OCT-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}.
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DR EMBL; CP013099; ALP53492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2TEG6; -.
DR STRING; 1748243.Tel_10240; -.
DR KEGG; tee:Tel_10240; -.
DR Proteomes; UP000055136; 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 CDD; cd03278; ABC_SMC_barmotin; 2.
DR Gene3D; 1.10.287.1490; -; 1.
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.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000055136}.
FT DOMAIN 521..623
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 443..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 300..362
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 657..929
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 1169 AA; 133114 MW; 6D1A7C81B1CAAE82 CRC64;
MRLKKIKLAG FKSFVDPTTI PLPSNMVGIV GPNGCGKSNT IDAVRWVMGE SSAKNLRGDS
MSDVIFNGST ARKPVGQASV ELVFDNTEGR LGGEYAQYNE ISIKRQVTRD GQSNYYLNST
KCRRRDITDI FLGTGLGPRS YAIIEQGTIS RLIEAKPEDL RVFIEEAAGI SRYKERRRET
ENRIKHTREN LERIDDLREE LEKRLATLQR QAKTAEKYKA YKEDERKLKA ELLALKFANL
EATVKERDKQ IQAQETALEG QVAEQRGLEA AIESQREHQV ESNERFNEVQ GRYYAIGSEI
ARLEQTIQHV RDTRQQQERE MGEVEEAWRE ATEHLSNDRD AIDELKMSLE SLEEESLVAR
EKESESALVR DGAEEEMQTW QQQWDEFNQT SSEHIRSAEV EKTRIQHQEQ SLAQVNQRMQ
RMEDELGLLS PGSLEGEIAE LSQAREQSEE QLGQLHHESE QQAEQIRYER EHTQALSGEL
DAERGRLQSM QGRRASLEAL QQQALGKDDH TLNDWLKRKG LDDAARLAQN IDVESGWEKA
VETALGLHLE SVCVEGMEAV ADALSDLDKG ALSLFDTGMD AGQVETGGAG TPLLDKVRCA
YSMASLLSGV YAAETLEQAL ALRSQIKASE SIVTRDGVWL GRDWLRVSRG VDEKAGVLQR
EQELKSLQSE IEETAERVDE LQAKLQQSRT RQQALERAQE ELQGTLRQVT QSKSGIESQL
SARQERMQQF HSRKQRLEGD IVDLRQQRQD MEASLAEARA RLDEILAKTE NFEQTRHELQ
QRRDALRQRL EQSRQQARAD RDRAHELALK LQSLRAQLEG TQQRLERMQG QLSHLERRRE
ELQAQLRSEG DPVADMTQEL EEKLAKRLGV EEELQQARRA MEEIDHTMRE LADERNQAEQ
RSQEIRSQLE KLRMASQEYR VRCQTVQEQF AETGFVMDEV RQGLPDAAQE AQWQEQVNEI
GQRIQRLGAI NLAAIEEFEE QSERKNYLDK QNADLIDALT TLENAIRKID KETRTRFKDT
FDKVNDGVKE LFPRLFGGGH AYLELTGEDL LDTGVAVMAR PPGKRNSSIH LLSGGEKALT
AVALVFSIFQ LNPAPFCMLD EVDAPLDEAN VGRFCTMVKE MSEKVQFIFI THNKTTMEMS
DHLAGVTMHE PGVSRMVAVD VDEAVRMVG
//
