ID I7IV85_9LACO Unreviewed; 1184 AA.
AC I7IV85;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=BN55_03580 {ECO:0000313|EMBL:CCI81003.1};
OS Lactobacillus hominis DSM 23910 = CRBIP 24.179.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423758 {ECO:0000313|EMBL:CCI81003.1, ECO:0000313|Proteomes:UP000009320};
RN [1] {ECO:0000313|EMBL:CCI81003.1, ECO:0000313|Proteomes:UP000009320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.179T {ECO:0000313|Proteomes:UP000009320};
RA Cousin S., Ma L., Bizet C., Loux V., Bouchier C., Clermont D., Creno S.;
RT "Draft Genome Sequence of Lactobacillus hominis Strain CRBIP 24.179T,
RT isolated from human intestine.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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:CCI81003.1}.
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DR EMBL; CAKE01000001; CCI81003.1; -; Genomic_DNA.
DR RefSeq; WP_008469596.1; NZ_CAKE01000001.1.
DR AlphaFoldDB; I7IV85; -.
DR STRING; 1423758.FC41_GL000235; -.
DR GeneID; 82846284; -.
DR PATRIC; fig|1423758.3.peg.239; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000009320; 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; 1.10.287.1490; -; 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:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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; 1.
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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}.
FT DOMAIN 514..635
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 764..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 318..359
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 416..492
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 1184 AA; 133537 MW; E6AB4A816C325CB8 CRC64;
MPLKQLILNG FKSFADKTTI NFDTGITGIV GPNGSGKSNI TEAIRWVMGE GSAKSLRGEN
MKDVIFAGSE FRAPLNRAEV SLIFDNQDKQ LNFDNKQVAV TRRILRSGDS EYLINNQQVR
LKDIRDLFVD SGLSQDSLAI ISQGKVDQIL NSRPEDRRGI FEEAAGVLHF KQQKEVALRQ
LDKTNENLIR INDLVKELED RVEPLHEQSS LAKEYKFEKS QLDSKLKKLL ALQIQNLDKQ
KRDLKQKADQ NKAILNKLDQ EVQTSQQDLE AKKEVSKALH AQKDNQQKSL LSLTQKIASL
NTDLQMSQQS REYDAATRKE YLAQKSELSA QKSELDQELA EIQATIDKQK NVLAKLDEKK
QKISSSLKQD PASLNKQLDD ARSRYIDLLQ EQTSTNNQIV YLENEIKRLN APKSEDQHLR
EELTQAQELL AQYKDQGKKL VTQRQALKAE IETLNQKVTQ QTKRLDDLNT LIQQTQANIA
RQNAQLDGLK RLQNRHEGYY YGVKYVLNHL EQFSGVIGVI GELISFPADL EAALTTALGA
GVQDLVARDR ESAKDAISLL KTSHAGRATF LPLDSLRQHT VAQSTITTLK AIDGFIGVAS
QLVSTKGSAD ISNAINYLLG NVLVAKDMNT ALRIQNCTGH YYRIVTLDGD IISPGGSMTG
GARNQRSNSP LQMNAELESL EQNIAKHQKQ LAEYQKQLAD FEKNSDNQAL NDKQSMLQEL
NQKISEQAIR FQNQEKETKR LERLDDLQKQ AHKRQVDELN KLSNQLQEKK DKKESLNTQA
NEQKAKMDDL KKTLENVDQA YAKLQNDLAE INSEIAVAKN KQANSKERFS QVQKQVKNNA
SQLSDLENKL SGLDQARDSS ASQEEINEQI ESLNQEKAEL TKKLAASNQN LGKIDAQINH
LESVASRNYD LRKDAAEDQE ALSVELSQFT SQINSKLRHL SQDYSLTYEA AIALTDGKND
LETRQNLEKE VKLHKMSIED IGPVNLQSIE EYEDVKTRYD FLNGQQNDLL KARSDIQESM
SKLDDEVRQR FDKTFKAVEK KFEDIFPIMF GGGKAKLVLT QPDDLLMTGI EIIAQPPGKK
LQRLSLLSGG ERALTAITLL FAMLEVNPVP FCILDEVEAA LDEANVDRFA KFLNHYDLHT
QFIVITHRRG TMQKADNLYG VVMQESGVSQ VLSVSLKDVK QEVN
//
