ID   SMC_MYCPA               Reviewed;        1196 AA.
AC   Q73VM3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=MAP_2990c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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=AAS05307.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE016958; AAS05307.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_040963272.1; NC_002944.2.
DR   AlphaFoldDB; Q73VM3; -.
DR   SMR; Q73VM3; -.
DR   STRING; 262316.MAP_2990c; -.
DR   PRIDE; Q73VM3; -.
DR   EnsemblBacteria; AAS05307; AAS05307; MAP_2990c.
DR   KEGG; mpa:MAP_2990c; -.
DR   PATRIC; fig|262316.17.peg.3167; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_11; -.
DR   Proteomes; UP000000580; 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   SMART; SM00968; SMC_hinge; 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..1196
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409277"
FT   DOMAIN          510..621
FT                   /note="SMC hinge"
FT   COILED          168..288
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          327..497
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          654..829
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          972..1026
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   1196 AA;  129070 MW;  E39E6CE0AA46EFE8 CRC64;
     MYLKSLTLKG FKSFASPTTL RFEPGITAVV GPNGSGKSNV VDALAWVMGE QGAKTLRGGK
     MEDVIFAGTS SRAPLGRAEV TVTIDNSDNA LPIEYSEVSI TRRMFRDGAS EYEINGSSCR
     LMDVQELLSD SGIGREMHVI VGQGKLDEIL QSRPEDRRAF IEEAAGVLKH RKRKEKALRK
     LDAMSANLAR LTDLTTELRR QLKPLGRQAE VARRAQTIQA DLRDARLRLA ADDLVNRRGE
     REAIFEAEAA MRREHDEASA RLAVASDELA AHEKALGELS GRAESVQQTW FALSALAERV
     AATVRIASER AQHLDLEPVT TGDTDPDALE AEAERVAAAE QQLLAELATA RSRLETARAE
     LAEREREAAE ADRAHMAAVR AEADRREGLA RLAGQVETMR ARVESIDDSV ARLSERIEAA
     AARAQQAKAE FETVQGRVGE LDQGEVGLDE HHERTVAALR LADERVAELQ AAERDAERKV
     ASLRARIDAL AVGLERKDGT AWLTENHSGA GILGPMAKLV KVRSGYEAAV AAVLGSAADA
     LAADGLGAAR SALGALKQAD GGRAALVLGD WPADPPAPQP APAGALWALD LIDAPERLRG
     AITAMLSGVA VVDDLDRALA LVAEHPRLRA VTLDGDLVGA GWVSGGSDRK LSTLEVTSEI
     DKAGAELAAA EAQVAQLSAA LSGALAEQAA RQDSAEQALA ALNESDSAIS GMYEQLGRLG
     QEARTSEDEW SRLLRQREEL EAGRTQTVAE VTELENRLRN AQETPQEPAA EPVNRQQIAA
     ATDAARSAEV EARLAVRTAE ERANAVRGRA DSLRRAAAAE REARVRAQQA REARLRAAAV
     AAAVADSGRL LATRLNAVVA AASRIRDALA AERQQRATAM AAVRDEVNAL SARVAALTDS
     LHSDEVANAQ AALRIEQLEQ MVLEQFGMAP ADLIAEYGPH IALPPSELEM AEYEQAKERG
     EQVFAPAPIP FDRPTQERRA KRAERELAEL GRVNPLALEE FAALEERYNF LSTQLEDVKA
     ARKDLLGVVD EVDARILQVF SEAYTDVERE FSDVFGVLFP GGEGRLRLTD PSNMLTTGIE
     VEARPPGKKI TRLSLLSGGE KALTAVAMLV AIFRARPSPF YIMDEVEAAL DDTNLRRLIS
     LFELLRARSQ LIIITHQKPT MEVADALYGV TMQGDGITAV ISQRMRGQQV DQLVTT