SCPA_BACSU
ID SCPA_BACSU Reviewed; 251 AA.
AC P35154;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Segregation and condensation protein A;
GN Name=scpA; Synonyms=ypuG; OrderedLocusNames=BSU23220;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT "The organization of the Bacillus subtilis 168 chromosome region between
RT the spoVA and serA genetic loci, based on sequence data.";
RL Mol. Microbiol. 10:385-395(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INTERACTION WITH SCPB AND SMC.
RX PubMed=12065423; DOI=10.1093/emboj/cdf314;
RA Mascarenhas J., Soppa J., Strunnikov A.V., Graumann P.L.;
RT "Cell cycle-dependent localization of two novel prokaryotic chromosome
RT segregation and condensation proteins in Bacillus subtilis that interact
RT with SMC protein.";
RL EMBO J. 21:3108-3118(2002).
RN [4]
RP CHARACTERIZATION, AND INTERACTION WITH SCPB.
RX PubMed=12100548; DOI=10.1046/j.1365-2958.2002.03012.x;
RA Soppa J., Kobayashi K., Noirot-Gros M.-F., Oesterhelt D., Ehrlich S.D.,
RA Dervyn E., Ogasawara N., Moriya S.;
RT "Discovery of two novel families of proteins that are proposed to interact
RT with prokaryotic SMC proteins, and characterization of the Bacillus
RT subtilis family members ScpA and ScpB.";
RL Mol. Microbiol. 45:59-71(2002).
RN [5]
RP SUBCELLULAR LOCATION, HOMODIMERIZATION, AND INTERACTION WITH SMC AND SCPB.
RX PubMed=12897137; DOI=10.1128/mcb.23.16.5638-5650.2003;
RA Volkov A., Mascarenhas J., Andrei-Selmer C., Ulrich H.D., Graumann P.L.;
RT "A prokaryotic condensin/cohesin-like complex can actively compact
RT chromosomes from a single position on the nucleoid and binds to DNA as a
RT ring-like structure.";
RL Mol. Cell. Biol. 23:5638-5650(2003).
CC -!- FUNCTION: Participates in chromosomal partition during cell division.
CC May act via the formation of a condensin-like complex containing Smc
CC and ScpB that pull DNA away from mid-cell into both cell halves.
CC -!- SUBUNIT: Component of a cohesin-like complex composed of ScpA, ScpB and
CC the Smc homodimer, in which ScpA and ScpB bind to the head domain of
CC Smc. The presence of the three proteins is required for the association
CC of the complex with DNA.
CC -!- INTERACTION:
CC P35154; P35154: scpA; NbExp=4; IntAct=EBI-2121359, EBI-2121359;
CC P35154; P35155: scpB; NbExp=5; IntAct=EBI-2121359, EBI-2121445;
CC P35154; P51834: smc; NbExp=20; IntAct=EBI-2121359, EBI-2121372;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12897137}.
CC Note=Associated with two foci at the outer edges of the nucleoid region
CC in young cells, and at four foci within both cell halves in older
CC cells.
CC -!- SIMILARITY: Belongs to the ScpA family. {ECO:0000305}.
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DR EMBL; L09228; AAA67487.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14254.1; -; Genomic_DNA.
DR PIR; S45549; S45549.
DR RefSeq; NP_390203.1; NC_000964.3.
DR RefSeq; WP_003246108.1; NZ_JNCM01000036.1.
DR PDB; 3ZGX; X-ray; 3.40 A; C/Z=1-86.
DR PDB; 5H66; X-ray; 1.82 A; C=176-251.
DR PDB; 5H67; X-ray; 2.07 A; C=176-251.
DR PDB; 5XG3; X-ray; 3.50 A; C/D=167-251.
DR PDBsum; 3ZGX; -.
DR PDBsum; 5H66; -.
DR PDBsum; 5H67; -.
DR PDBsum; 5XG3; -.
DR AlphaFoldDB; P35154; -.
DR SMR; P35154; -.
DR DIP; DIP-52200N; -.
DR IntAct; P35154; 15.
DR STRING; 224308.BSU23220; -.
DR PaxDb; P35154; -.
DR PRIDE; P35154; -.
DR EnsemblBacteria; CAB14254; CAB14254; BSU_23220.
DR GeneID; 938950; -.
DR KEGG; bsu:BSU23220; -.
DR PATRIC; fig|224308.179.peg.2529; -.
DR eggNOG; COG1354; Bacteria.
DR InParanoid; P35154; -.
DR OMA; YLVMAAM; -.
DR PhylomeDB; P35154; -.
DR BioCyc; BSUB:BSU23220-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.580; -; 1.
DR HAMAP; MF_01805; ScpA; 1.
DR InterPro; IPR003768; ScpA.
DR InterPro; IPR023093; ScpA-like_C.
DR PANTHER; PTHR33969; PTHR33969; 1.
DR Pfam; PF02616; SMC_ScpA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW Reference proteome.
FT CHAIN 1..251
FT /note="Segregation and condensation protein A"
FT /id="PRO_0000211080"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:3ZGX"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3ZGX"
FT HELIX 39..73
FT /evidence="ECO:0007829|PDB:3ZGX"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 210..225
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:5H66"
SQ SEQUENCE 251 AA; 29612 MW; 9FE03F117D2919A0 CRC64;
MEEYQVKIDT FEGPLDLLLH LINRLEIDIY DIPVAKITEQ YLLYVHTMRV LELDIASEYL
VMAATLLSIK SRMLLPKQEE ELFEDELLEE EDPREELIEK LIEYRKYKDA AKDLKEREEE
RQKSFTKPPS DLSEYAKEVK QSEQKLSVTV YDMIGAFQKV LKRKKINRPM ETTITRQDIP
IEARMNEIVH SLKSRGTRIN FMDLFPYEQK EHLVVTFLAV LELMKNQLVL IEQEHNFSDI
YITGSESIHG A
