ID G2FED5_9GAMM Unreviewed; 1169 AA.
AC G2FED5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
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:EGW54905.1};
GN ORFNames=TevJSym_ah00850 {ECO:0000313|EMBL:EGW54905.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW54905.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW54905.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:EGW54905.1}.
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DR EMBL; AFZB01000008; EGW54905.1; -; Genomic_DNA.
DR RefSeq; WP_006474451.1; NZ_AFZB01000008.1.
DR AlphaFoldDB; G2FED5; -.
DR PATRIC; fig|1049564.3.peg.1269; -.
DR eggNOG; COG1196; Bacteria.
DR Proteomes; UP000005167; 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; 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:UP000005167}.
FT DOMAIN 521..622
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 170..211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 244..379
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 405..486
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 663..942
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; 133110 MW; 1195041CFFCB5B55 CRC64;
MRLEKIKLAG FKSFVDPTTV PMPSNLVGIV GPNGCGKSNV IDAVRWVMGE SSAKMLRGES
MADVIFNGSS SRKPVGTATI ELLFDNAEGR AGGQYAQYNQ ISVKRQVSRD GQSNYYLNGT
RCRRRDITDL FLGTGLGPRS YSIIEQGMIS RLIEARPEQL RVYLEEAAGI SKYKERRRDT
ENRIRHTREN LERLEDLRGE VAKQLQHLQR QAATAEKYQS YKAEERQLKA ELLALRWRSL
DEELQQRDRS IAEMENRLEQ ALTEQRRLEA GIEAHREQHT EANDLFNEVQ GCFYAIGAEI
NGLEQSIQFA RDARRQQQQD LEQVEQTWQE SEAHRAQDQS RLEELNENLL REEPRLEEAQ
ALEEEAALAV ATAEEAMNAW QSQWEAFNQQ AAEPAQSAQV ERTRINNLEQ RERDQVRRLQ
RFDEELAGLD EGPLQQEIAD FERQQQEQQA RAEVVQEQLD QTMQQIGEQR DANRQLAQRL
DEVRAQLQGD KGRRASLEAL QQAALGKQGD ALSEWLEQSH LSRAARLAEQ LEVESRWQRA
VEIVLGFHLQ AVCVENLDDL KEALAGLQQG ALSLLDQTSV PPDAPEPPGD SLLGRIRSPW
PLQNLLGGVR LAEDLDTALM MRRGLRSGES VITPEGAWLG PNWIRLTREE DESTGVLARE
EELRRLSQLL EQGEANAAEL AEQSEQGSSE LQRIEQQREQ LQSSFNEINR TLSGIASALS
GKRTRAEHIN QRREQLHREQ QEILQQIETD REELELTRQR LHSALESIET LGNRRESLVV
ERDGLREALT QLRDRLNQQR AQSHQAALQI QSMRTAQQSL QQNLQRMSSQ LDHLAQRREE
LRGTLAAAET PLEQQGEALE EKLVQRLAVE KELSEVRASL ERVDQELREL EQQRQRIEQA
VQTRRSELDQ GRLQRQEVLV RCKTLEEQLR ETDQTAEALF REMPEEAAEG VWRERLEKLA
NRIQRLGAIN LAAIDEFKEQ SERLAYLDEQ HADISSALDT LEGAIRKIDR ETRTRFKETF
DKVNDGIKEL FPRLFGGGHA YLELTGEDLL DTGVTVMARP PGKRNSSIQL LSGGEKALTA
VAMVFAIFQL NPAPFCMLDE VDAPLDDANV GRFCQMVKAM SDKVQFIFIT HNKITMEIAN
QLSGVTMHEP GVSRLVTVDV EEAAQLTAV
//
