ID S6BDF8_9GAMM Unreviewed; 1166 AA.
AC S6BDF8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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:BAN69473.1};
GN ORFNames=EBS_1591 {ECO:0000313|EMBL:BAN69473.1};
OS endosymbiont of unidentified scaly snail isolate Monju.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN69473.1, ECO:0000313|Proteomes:UP000015562};
RN [1] {ECO:0000313|EMBL:BAN69473.1, ECO:0000313|Proteomes:UP000015562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Monju {ECO:0000313|EMBL:BAN69473.1};
RX PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., Watanabe T.,
RA Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., Nemoto S.,
RA Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT "Allying with armored snails: the complete genome of gammaproteobacterial
RT endosymbiont.";
RL ISME J. 8:40-51(2014).
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; AP012978; BAN69473.1; -; Genomic_DNA.
DR RefSeq; WP_043108205.1; NZ_AP012978.1.
DR AlphaFoldDB; S6BDF8; -.
DR STRING; 1248727.EBS_1591; -.
DR KEGG; enm:EBS_1591; -.
DR HOGENOM; CLU_001042_2_2_6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000015562; 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; 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:UP000015562}.
FT DOMAIN 521..619
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 452..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..204
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 667..904
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 981..1008
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 1166 AA; 132058 MW; C825F88D3CDC7359 CRC64;
MRLEKIKLAG FKSFVDPTTV HFPSNLVGIV GPNGCGKSNV IDAVRWVMGE SSAKMLRGES
MADVIFNGSS TRKPVGMASI ELIFDNSDGS AGGQYAQYAQ ISVKRQVSRD GQSQYFLNGV
RCRRRDITDL FLGTGLGPRS YSIIEQGMIS RIIEARPEEL RVYLEEAAGI SKYKERRRET
ENRIRHTREN LERLDDVREE VQKQLCHLER QAATAEKYKT LKDEERRVRA ELLALRLSSM
QDDVAQRDRR INELETALEA AIARQREVEA EIEQQREAHG GANEHFNEVQ GRFYAIGSEI
ARLEEAIQYA REARRQQELD LQQAERALAE ARELGQQDQS RLQQLAEELE RDRPRLEEAR
MAEEAAREQL AAAEEAMAAW QAEWDRFNEQ VNEPAQQAQV ERTRINHFEQ QEQQLRRRIE
RNQEEQRRLS DIELEAEIRE LLRREEEAEA ALAEAREQTE QAREDIEQAR GEIQQRQDTL
DRLRSELQSL QGRLASLQAL QQAARGEDDE ALNDWLSRQG LEGARRLLEG IEVEGRWQQA
VEVALGQHLQ AVLVDDLASH AGDVEALLAA GARLFETREG QAAARPGTLA SVVRGPAGLI
GILNGIYLAD DLEQALTRRD ELGESESLIT PEGVLVGNGW LAAARGNEAE RGVLAREREI
RELSEREQEL APRIEELERL LAEARERLRQ AERAREEAQA RQDAGARALA DIKALLSGKQ
ARAEQIRQRL GGLEEEAAEL QQQLQEGAEQ IEAARERLHA ALARVDELDR RRESLQAERE
RLRQRLEEAR QAANARHAEV HELALRIESI RSTEDSLRSG IDRVHSQVAQ LEQRVAELRE
ALEQSKAPMG EQQIQLETQL QERVAVEARL AEARKALEGI DHRLRELEQS RHGVEQQVQE
TRIALDQARM ARQEIVVRAG TLREQLGETG FELAALLEEM PEGASVQAWQ ARAEQLTTRI
QRLGPINLAA IDEFREQSER MEYLDRQHED VTKSLETLEE AIRKIDRETR TRFKETFDKV
DTGFKELFPK LFGGGHAYLE LTGDDLLDTG VTVMARPPGK RNSSIHLLSG GEKALTAVAL
VFSIFRLNPA PFCMLDEVDA PLDDANVGRY SQLVKEMSEH VQFIFITHNK VTMEIANQLM
GVTMHEPGVS RLVSVDVEEA ASLAAV
//
