ID   SCPA_MYCPN              Reviewed;         506 AA.
AC   P75478;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Segregation and condensation protein A;
GN   Name=scpA; OrderedLocusNames=MPN_300; ORFNames=MP536;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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 highly related to the dihydrofolate
CC       reductase family in its N-terminus. It is however unknown whether it
CC       contains such enzymatic activity. {ECO:0000305}.
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DR   EMBL; U00089; AAB96184.1; -; Genomic_DNA.
DR   PIR; S73862; S73862.
DR   RefSeq; NP_109988.1; NC_000912.1.
DR   RefSeq; WP_010874657.1; NC_000912.1.
DR   AlphaFoldDB; P75478; -.
DR   SMR; P75478; -.
DR   IntAct; P75478; 5.
DR   STRING; 272634.MPN_300; -.
DR   EnsemblBacteria; AAB96184; AAB96184; MPN_300.
DR   KEGG; mpn:MPN_300; -.
DR   PATRIC; fig|272634.6.peg.324; -.
DR   HOGENOM; CLU_538423_0_0_14; -.
DR   OMA; DDELYIC; -.
DR   BioCyc; MPNE272634:G1GJ3-469-MON; -.
DR   Proteomes; UP000000808; 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..506
FT                   /note="Segregation and condensation protein A"
FT                   /id="PRO_0000211097"
FT   DOMAIN          1..166
FT                   /note="DHFR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT   REGION          167..506
FT                   /note="ScpA"
SQ   SEQUENCE   506 AA;  59521 MW;  578FA071E57CD6CF CRC64;
     MITLIWCQDK HFGIGRDNTI PWKLTEANQH FYNTTKNQTV VMGYNTFQEL GDKLTDHNVV
     VLSKKHFEEL QNNTNIKVFN SIEKLLQHHF NRDLYVIGGK QIFHHFIELA DRLIISVLPV
     DFKCNLRLKL GLDSFELMQE QQHSQFKVQY WHKKHPERLS FNVFLEDYNG TLPNLLELLI
     DKKFNLHQVD IAKITTQYLH LINTNLNKQA IEPITDYLVI TSRIVEQKAN NLLQINDIAL
     DSDFLDNKLR DKLVAQLVEY KRYRESLDDF EKLRINRLAY FSKDNDFNRF IQTVDKSNTE
     PVKIEDELPN YVSVLKLHHA MNKLMQRWRA QFLANKNISI QELSIEQVQA EILATIKQFG
     YHSVSLKRVL LKVNHHISLM YFITAFVALL VLINNQIIDI EQTSFDDELY ICLLDSSRIE
     QLQETPEAMV ERAVKQRQEA QELARQVARE KAIANAQKRE AYLKAKYGKD YLTREQFLKL
     SPEERAAHVA KMKQLKLVKN DNGRDN