ID M7MXW7_9BACT Unreviewed; 1178 AA.
AC M7MXW7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:EMR01268.1};
GN ORFNames=ADICEAN_03617 {ECO:0000313|EMBL:EMR01268.1};
OS Cesiribacter andamanensis AMV16.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC Cesiribacter.
OX NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR01268.1, ECO:0000313|Proteomes:UP000011910};
RN [1] {ECO:0000313|EMBL:EMR01268.1, ECO:0000313|Proteomes:UP000011910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMV16 {ECO:0000313|EMBL:EMR01268.1,
RC ECO:0000313|Proteomes:UP000011910};
RX PubMed=23682146;
RA Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL Genome Announc. 1:E00240-13(2013).
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:EMR01268.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AODQ01000130; EMR01268.1; -; Genomic_DNA.
DR RefSeq; WP_009196997.1; NZ_AODQ01000130.1.
DR AlphaFoldDB; M7MXW7; -.
DR STRING; 1279009.ADICEAN_03617; -.
DR PATRIC; fig|1279009.4.peg.3660; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000011910; 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; 3.30.70.1620; -; 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; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011910}.
FT DOMAIN 520..632
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..215
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 297..485
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 671..787
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 879..934
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 1178 AA; 134324 MW; 0CB62065619253ED CRC64;
MRLTRLEIKG FKSFGDKVVI NFDEGITGIV GPNGCGKSNV VDAIRWVLGE QKTKALRSDK
MENVIFNGTK HRKPSQLAEV SLTFDNTKNL LPTEYSRVTI TRRYYRSGES EYELNGVACR
LKDISNLFLD TGIASNSYAI IELKMVDELL NDKEGSRRAL FEEAAGISKF KKRKKETLRK
LEETNADLER VKDLLFEIEK NLKSLERQAK QAERYFALKE DYKKLSLRLG RLAISQSTER
FLGLHKQLEA EQDRKGALDA QLAEREALAE ESKAQLLGRE KLLSSRQKTL NEHVSKIRQV
ESDKKIKNER LRFLNDKRDS LLEQLQSDKQ SYERAAFSLN GLAQERSEAE ALATEAKALL
DELREAHDEQ KSITTALREE AATATNQQRQ LQEQAFKLSK SLEIKQMQLS SLRQELEKTA
QEGSQHSNSL SQFEDKLADV QEAVAEKEQE LQQLQADEGQ MQQQLAELEQ GLNQNREALA
ADRRQLDARQ NEYNLTKSLV DNLEGFPEAI RYLKKKTDWG RNVPLLSDII TCSEAYRVAI
ETYLEPWMNH YVVDSWQQAQ EAIALLSEAA RGRAQFFVLE ALPPASPSPT TPPAGCTPAL
SVVEADPKYA PLTAHLFADT YLCEDAEMET IGSSAYSLIS RSGRIIKRRY SLLGGSVGMF
EGKRIGRAKN LEKLQKDIQQ LLSEVSRLEK LQQEQHTELG RLKSSTRRPQ IEAVSRELSL
LQQELVQVRT RHEQLLQLLS NQATRQDDMR QQMEVLQDEI ADIDPEAAAV AERLQALEAR
SIQLQDDLAY QNEALSVKSA RFNEQNLLYH QKENKLNSLV QEMGFKQQSL QSSEERISRN
KSSLADTEAE IEGLMQRGEL GDEELMAMYS EKESIEAGVN EAERDYYEMR GQIDALEKEA
RELQRRRESS QALMMELQNR QNEYKLQLTS VKERLAVEFN VDAEELMEAP AVDELLSEAE
LQQEVRQVRE KIDKIGPINP MAMEAYQEIQ ERYQFITAQR DDLVKAQESL LETMAQLDSA
AQEAFLSAFE QIKENFVKVF RSLFTEEDDC DLRLTDPSNP LETTIDIIAK PKGKRPLTIN
QLSGGEKTLT ATSLLFSIYL LKPAPFCIFD EVDAPLDDAN IDKFNNIIRK FSQDSQFIIV
THNKRTMAST DIMYGVTMLE MGVSRVVPVD LRELEVEF
//