SMC_HALMS
ID SMC_HALMS Reviewed; 1226 AA.
AC E1X022;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=BMS_3207;
OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS (Bacteriovorax marinus).
OC Bacteria; Proteobacteria; Oligoflexia; Bacteriovoracales;
OC Halobacteriovoraceae; Halobacteriovorax.
OX NCBI_TaxID=862908;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ;
RX PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA Williams H.N., Stine O.C.;
RT "A small predatory core genome in the divergent marine Bacteriovorax
RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL ISME J. 7:148-160(2013).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 SMC hinge
CC near the middle of the molecule. These domains are separated by coiled-
CC coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBW27958.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FQ312005; CBW27958.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044557708.1; NC_016620.1.
DR AlphaFoldDB; E1X022; -.
DR SMR; E1X022; -.
DR STRING; 862908.BMS_3207; -.
DR PRIDE; E1X022; -.
DR EnsemblBacteria; CBW27958; CBW27958; BMS_3207.
DR KEGG; bmx:BMS_3207; -.
DR PATRIC; fig|862908.3.peg.3064; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_7; -.
DR OMA; HNKIAME; -.
DR Proteomes; UP000008963; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1226
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409263"
FT DOMAIN 527..635
FT /note="SMC hinge"
FT COILED 173..231
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 269..491
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 679..741
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 775..965
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 1006..1078
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1226 AA; 140303 MW; 5B84D0C5C5369B9D CRC64;
MKLKRLVIQG FKSFKDRTTI HFDDGITGIV GPNGCGKSNI VDALFWVMGE QSAKHLRGKS
MKDLIFAGSS KYNPGAYAEA TLVLGNDDGK HIHIGNKVSS PSEIQLTRKL YRNGETEYRI
NNYPARLKDI QEVFMDTGAG AKSYSIIAQG EINRLVQAKP EERRTMIEEV AGITKFKVRK
KESLKKIEQT EQNLNRLQDL QSEIEKNLKA LQKQAEKAER ARSLKEKIKR NDIIVHAHKV
YDLLKDLRDG KTLLNEKTLE LEGWGTRKNS LEISLEEERF KKEEQTEKLE ILQKERNEIS
TQLATAEERF SNLCKTLTDK ENLIETRQKE MTELEEELVE REEKIKALED SLVELQTRNE
ETVNFEEVEE KIELLKERLE LKTDQVDTLK EEIELKKSEL NTLSQAAFQN TSKLEEYAAN
LQDITEEIEA LEKQYSGVST QIADERDAVH TAQELSEKLT EVESELKSEI EELISANKEL
DAKLKEKSKS LITKESKLSS LQEIAAAMDG VREGAVEFLE TVDSDKYQLL GNLIQCEEDH
AKAVQNLLSD FMDTLVSTDE DVSAVIEWCK TNNDKALEFL APNKNGDITS EETLERLRVA
TGGDITPVHE LLNLPEEYKS KLIPFFDGYF IASKFDQEVF KSISDSIRFK AISSTDGKLL
VKNPGNGKIL TMSGSSEGQG VVERNNQIQE LEKEIEVLRV EVAELETNSG EKSLVLEQKR
DSLEEQRNLL SEARADHAAK KSALESKLSG MESGNTRLEI LKKRKQEISK SRLDMLESED
SLSKNKSSLD EELEELSTRF EEENAELADL KSTYETEREA YMEKQVEINT FKERVSGIQS
QIEDINSQMD KQTARIASNK ELIEKYNEEI ETTNDQIDTL ESSNQEMASE LSERDDVLGI
MKDDLTQLLL AMQEREDEVK ELSKKIAKNE KDITEYELKI NQWQNDEVEV VKNIFEKYQI
DLREAIGGFL EYDQDDFDDL IDTRQMHFME TENGLVTIEK QSYEFHRRYG QDLKECSNKL
KNYKNEYNRL GEINWQAIED YDRQKLRFDF LRVQEVELKQ SLEDLETAIN HIDEKSKERF
KIAFEEVDVR FRKVFPIIFG GGEAMLKVTG DINDSECGVD IIAKPPGKKM QNINLMSGGE
KAMTAVSLIF SIFLVKPSPF CLLDEVDAPL DDANVGRFNE LLREMSSDSQ FILITHNKKT
MELNDTLYGV TMQEPGVSKA VSVQLH
