ID F9VCV8_LACGL Unreviewed; 1172 AA.
AC F9VCV8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=LCGL_0699 {ECO:0000313|EMBL:BAK60159.1};
OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK60159.1, ECO:0000313|Proteomes:UP000008520};
RN [1] {ECO:0000313|EMBL:BAK60159.1, ECO:0000313|Proteomes:UP000008520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK60159.1,
RC ECO:0000313|Proteomes:UP000008520};
RX PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT "Complete genome sequence and comparative analysis of the fish pathogen
RT Lactococcus garvieae.";
RL PLoS ONE 6:E23184-E23184(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}.
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DR EMBL; AP009333; BAK60159.1; -; Genomic_DNA.
DR RefSeq; WP_014024547.1; NC_017490.1.
DR AlphaFoldDB; F9VCV8; -.
DR STRING; 420890.LCGL_0699; -.
DR KEGG; lgv:LCGL_0699; -.
DR PATRIC; fig|420890.5.peg.695; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000008520; 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; 1.20.1060.20; -; 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; 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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000008520}.
FT DOMAIN 520..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 176..203
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 229..287
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 436..473
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 677..970
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 1172 AA; 132616 MW; 01C85BB3347A03AD CRC64;
MYLKKMEIVG FKSFADRTKI EFDQGVTAVV GPNGSGKSNI VEALRWALGE QSAKSLRGGK
MPDVIFSGTA KRKALNYTEV IVTFDNTDQY LTGYEEDAEV TITRRLYRNG DSEFLINGRK
CRLKDIHELF TDTGLGRDSL SIISQGRIES VFNSKAEERR AIFEEAAGVL KYKTRRTETE
SKLQTTQDNL DRLEDIIFEL NGQLTPLRAQ RDVALCFQDL EAQRSELALS VLVAQLLDEK
KKYEQAKEDL NTAETELSAL KSQQEGYEAQ LTHLKKARLK VEQEQEKVQG DSLSLTELKS
DLQHKIEVFD LQKSSSQKSA AERQARIEEL DAKLLEVSQK KEASEKKKAE LKDKEHEAQE
QLEQLEKELA RFAESPESLA ERLREDYLQL VQQEAEFSNQ LTKNKAEYEN ISRRLVESDE
NAKENTEKFQ TISADLTKTE AALDTLTQTV RELEKELQEK TAAEAKYVEA ERQGQNVMYD
QMQQLSKYKA NLASMENIRD SHSNLYQGVR AVMTQSVALG GIVGVVADLL TFDKKYTTAI
DIALGGGSQN IVVEDENSAK KAIAYLREKR LGRATFLPLT TIKPREFRNY ERLVTMEGFI
DTALNLVSFE PRLQRAMSSL LATTAIVDTA EHASQIARAM NYTIRIVTLD GTQINPGGSY
SGGAAKRNNT TFTSTEIEHL TEVIALAESK LKAVEDILQK QQLTRQTLSE QVEALRSNIQ
EKRLAEQSLQ LQIKQLSEQK TNLQALVADT ENTEAHQALQ ELSENNEKLG QQLSKIAEDK
QSLDDQLEEV KSNSQSFNAL KEQKNSAYHE TKLLLSSLKN ELRFAQTEQE RLTQEYETLG
TEKAKLQASG EARIDEASRN LYAQQLKETE AKLQEANVKL VSLRFERDDL QAQTEEFEEQ
NRDLLEQNQV LNNQKARLEV RIEQSEKLLK NRQNTLFTEY EMSFDEAKMK AKTLEDLSES
EQQLSLLERQ IRALGPINLD AITQYEEVHQ RHAFLSGQRD DLLEAKNMLL ETIQEMNDEV
EIRFKTTFEQ IRESFQLTFS QMFAGGEADL ELTSTNLLEA GVEIKVQPPG KKLASLNLMS
GGEKALTALA LIFAILRVRT VPFVVLDEVE AALDEANVKR FGDYMNHFDN SNQFIVVTHR
RGTMAAAGTM YGVTMADAGV SKVISVRLED EV
//
