ID V5RJC9_SPIAP Unreviewed; 983 AA.
AC V5RJC9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, 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:AHB36664.1};
GN ORFNames=SAPIS_v1c08190 {ECO:0000313|EMBL:AHB36664.1};
OS Spiroplasma apis B31.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276258 {ECO:0000313|EMBL:AHB36664.1, ECO:0000313|Proteomes:UP000018550};
RN [1] {ECO:0000313|EMBL:AHB36664.1, ECO:0000313|Proteomes:UP000018550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B31 {ECO:0000313|EMBL:AHB36664.1};
RX PubMed=24407648;
RA Ku C., Lo W.S., Chen L.L., Kuo C.H.;
RT "Complete Genome Sequence of Spiroplasma apis B31T (ATCC 33834), a
RT Bacterium Associated with May Disease of Honeybees (Apis mellifera).";
RL Genome Announc. 2:e01151-13(2014).
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; CP006682; AHB36664.1; -; Genomic_DNA.
DR RefSeq; WP_023789977.1; NC_022998.1.
DR AlphaFoldDB; V5RJC9; -.
DR STRING; 1276258.SAPIS_v1c08190; -.
DR KEGG; sapi:SAPIS_v1c08190; -.
DR PATRIC; fig|1276258.3.peg.840; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_14; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000018550; 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 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 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; 2.
DR PIRSF; PIRSF005719; SMC; 3.
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|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000018550}.
FT DOMAIN 417..536
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 170..211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 319..395
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 598..724
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 983 AA; 111673 MW; ED833CFA30887B32 CRC64;
MIFLKRIEAF GFKSFAEPTT LNYGYAMTGI VGPNGSGKSN ITDAIMWALG EQSSKSLRGD
SMEDIVFSGS SEHKALNMAE VTLVFDNSTR AFSSLEYNEV SITRKYFKLN KESEYYINGT
RVRLKDIQDV ALETGLTKSS LAIISQGSIS SFVESSPEQR RRLFDEAAGV ARYKKRKEEA
LRKLIRSQEN LDRLNDIINE IERKLPSLKR QSSKALEYQK KWEELKNIEV SILVKDIQLY
KKRILEIDEE KLNLKSKISS LDKNIVIKAE EFNNLNKKSF MNEKELASLN KEFTEIVDNI
GKLRISKINL ESKKSKLDID EKEFRISELK NKSKEYEVKL NSEEQKLARL LNEKQDKKKL
VDSLSKERFD FNNKLDLLRK EITKIEILLE NINNKKNSLE GYFEGVKNVL ENKKTLNGII
GTVQEIISID QEHELAMSSI LQNSVQNIVA TTANDVKQAI NFLKSNKAGY ATFLPLDTLK
PNLISGEKKF AIQNANGFLG FANELIKTNK KYQVVLDYLV GSFIVVDNYD NAVELAKLIN
YKFNIVTLDG ERILPHGAIV GGSRKIKSTL TFDASKLTEL EKSKLSLDHE ESSIVKKIAL
INEKIELLRE ELTETQSSIG AAKKASEHYE KEISDVKEEY RILTGKELNS NVDLVQSIDE
QIIEVVEKIS QLESKKEEIN QKINVIRSVK DKSVEKQNDL NLTIDEERKM LQRLKDNYSS
LSTDRLLLFE KQSNLTERLG QNYNLTFESA IELEKVAILD EDETRKKINL LRSEIKSLGN
INVDAIQEYE EENKRYQNYV EQTNDVQESI GSLKTAINDM DIQMTTQFKT IIKQVNDALP
KTFATLFGGG TASIVYTTPN DILNSGIDIK ISPPGKKISN LNLLSGGEKS MVALSVLFSI
LKVKPIPLVI LDEVEAPLDI ANVERFAKYI KTFTENTQFM IVTHRIGTME NCDILFGATM
QQKGITKLVQ IKLLEARKLS NSN
//
