ID A0A292RGW9_9BACT Unreviewed; 1169 AA.
AC A0A292RGW9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:DAA97408.1};
GN ORFNames=CPT80_02065 {ECO:0000313|EMBL:DAA97408.1};
OS Candidatus Gastranaerophilales bacterium HUM_9.
OC Bacteria; Candidatus Melainabacteria; Candidatus Gastranaerophilales.
OX NCBI_TaxID=1916320 {ECO:0000313|EMBL:DAA97408.1, ECO:0000313|Proteomes:UP000218540};
RN [1] {ECO:0000313|EMBL:DAA97408.1, ECO:0000313|Proteomes:UP000218540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HUM_9 {ECO:0000313|EMBL:DAA97408.1};
RX PubMed=28360330; DOI=.1126/science.aal3794;
RA Soo R.M., Hemp J., Parks D.H., Fischer W.W., Hugenholtz P.;
RT "On the origins of oxygenic photosynthesis and aerobic respiration in
RT Cyanobacteria.";
RL Science 355:1436-1440(2017).
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 Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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}.
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:DAA97408.1}.
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DR EMBL; DABG01000006; DAA97408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292RGW9; -.
DR STRING; 1916320.GCA_002103075_00330; -.
DR Proteomes; UP000218540; 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 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; TIGR02169; SMC_prok_A; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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.
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}.
FT DOMAIN 516..631
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 161..222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 327..452
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 663..898
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 951..1013
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; 133962 MW; 32DAF16E21F6AB8E CRC64;
MYIKQIEIDN FKSFATKIEI PLLKGFSTIV GPNGSGKSNI IDAVLFALGL ATSRNLRAEK
IADFISTYTK RNEAIVKVTF ADGENGEEFS VARKIKKSTQ GYNSVYYLDD KITTHTEILM
KLEKYNVTPN SYNVVMQGDV TSIIGATDNE RRKIIDEIAG VAEFDRQINQ ASEKLDAVEV
SVKNSSIMLH EVENRLNQLK EEKEVALKYQ KLKDEKHGLE SQVNTVKFFD IKTKLEQAHE
NILEYTKKKK LEEVNAKDLD ERIKVIDEKY QEICETVKEK GEAHQIEVQK KAEECKGEIS
RKENSFNFEE KQIQDKKKTI ENSINGIDNH NTKIEVANQN IKSKQVDISV TDKELEKQRA
ERKRITEDLT GLNENVDQQI KHREHLRKEL DTLKDKETAL IQKQVPLETE LQNLNNKIKD
AKQGIETYNS LKNDYESKKD SLELQIETLK KEQQDCKIIQ QNITHDYDKV INELTDLDFE
LSAGRKQLFN LEVRKNASEV SSGNRAIQTV ENAHIEGVHA PLFKLGNVDK EYATALEVAV
GGRMSNIVVD DPDTATTVFE VVRSSGAGRV TCIPLNKIAE APNSLNLPRE QGVIDYAINL
IDFDDMYLDA FYYAVGSTLV VENDYVAKKL IRKYRMVTLD GTLYEKTGAM TGGGKVTTNL
KFSIHEDDEL EKYKKRLQEI ENKYNKAKQR KQELETKREQ VRINYSNAMT EFNKANIELN
SLNKNFETSK TTYAQNQEFI KLSEPEIERI NKELDKSEER HIKLIDEMTE LKSKIEEIEQ
LLDDSDLKKL KEMTEGIDSE IARLETNKRN FENEIQSFNM EIAFHKTTIE NSKETIEKCK
SDIEESERNK LLFTEDIKKL KVQLEDYETQ IEEIKEKLGD LLKQRDEINE QLIDLRTKKN
VKTAELEKIA EQIESFKARR REIEPELEVA RKDLEEAGVE ISKLQPVNMS IDELNSKIQR
LSRKMDDLGA VNMNAITQYD EVSQREQELK EKIETLSHER QEIINRMNGY EQVKKDAFMT
TYNNINSNFK ELYHQLSGGE GSLILEDEVN PFAGGLDIEA KPGDKPKVKL KGLSGGEKSV
AALALVFAIQ KYMPAPFYAL DEVDSALDPI NIDKLANMIK TQAKQIQFVV VTHRKPMIEV
SDRSIGVTQK EKGKSLVSGV THHKQEIVV
//