ID   SCPA_MYCGA              Reviewed;         592 AA.
AC   Q7NB76;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Segregation and condensation protein A;
GN   Name=scpA; OrderedLocusNames=MYCGA4030; ORFNames=MGA_0037;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(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 (By
CC       similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated with two
CC       foci at the outer edges of the nucleoid region in young cells, and at
CC       four foci within both cell halves in older cells. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ScpA family. {ECO:0000305}.
CC   -!- CAUTION: Fused to a domain related to the dihydrofolate reductase
CC       family in its N-terminus. It is however unknown whether it contains
CC       such enzymatic activity. {ECO:0000305}.
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DR   EMBL; AE015450; AAP56753.2; -; Genomic_DNA.
DR   RefSeq; WP_011113649.1; NC_004829.2.
DR   AlphaFoldDB; Q7NB76; -.
DR   SMR; Q7NB76; -.
DR   PRIDE; Q7NB76; -.
DR   KEGG; mga:MGA_0037; -.
DR   PATRIC; fig|233150.7.peg.453; -.
DR   HOGENOM; CLU_538423_0_0_14; -.
DR   OMA; DDELYIC; -.
DR   OrthoDB; 710856at2; -.
DR   Proteomes; UP000001418; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
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-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR   CDD; cd00209; DHFR; 1.
DR   Gene3D; 3.40.430.10; -; 1.
DR   InterPro; IPR024072; DHFR-like_dom_sf.
DR   InterPro; IPR001796; DHFR_dom.
DR   InterPro; IPR003768; ScpA.
DR   PANTHER; PTHR33969; PTHR33969; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   Pfam; PF02616; SMC_ScpA; 1.
DR   SUPFAM; SSF53597; SSF53597; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW   Reference proteome.
FT   CHAIN           1..592
FT                   /note="Segregation and condensation protein A"
FT                   /id="PRO_0000211093"
FT   DOMAIN          1..155
FT                   /note="DHFR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT   REGION          156..592
FT                   /note="ScpA"
SQ   SEQUENCE   592 AA;  70351 MW;  1585640A8DD72112 CRC64;
     MIKLIWCEDL NHGIAKNNQI PWKIDEELNH FHQTTTNHPI IMGYNTYLAM NKILANQANI
     VISKKHQREL KNKNELFLYS DLKKALIDFS IVDLFIIGGK KTIEQAIKYA DQLVISKLNA
     DYGCDLFVNL NYDDFSLVQT KEYDQFVVEY WERKPNTKKP EDLIEELNIN LNDDFLNLSF
     KHFSGPFDLL LHLIKDKKMD IMALDLFELT NQYFAYINKH MINLDLVSDY LYMACELLRI
     KSDLSIPNFE DETKIDLNND DERDRIVKRI IEYKRYSELL PSLQKMQLER FSLFAKEEDD
     WDVFKLTSND LLEAPLPDYV NPKKLKKAME RVFEKLKIKT ITEHKIVIEE LSIEDVKNEI
     LSIIKKLLNN QYDRFIDLEK IFEQIDPKKL NLRYFVTSFV CLLILVREQK IDLNQKNDDE
     SISACLVDPT KIVNSQESIQ EVIQRQQEDE KALKESIKQI QEERKQSFFK QREEYLKKKY
     GEYYVSREQY QKLTPEEKIN IRINQRKIDE QEKLNKAKAQ NLVDENNQII DLKTKKPSAK
     QILYEADLII KQLDDLINDQ QEDYDSQAEL EALHTDLIKL DDEQEQDLIK EE