ID   MINC_SALPA              Reviewed;         235 AA.
AC   Q5PI83;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Probable septum site-determining protein MinC {ECO:0000255|HAMAP-Rule:MF_00267};
GN   Name=minC {ECO:0000255|HAMAP-Rule:MF_00267}; OrderedLocusNames=SPA1059;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Cell division inhibitor that blocks the formation of polar Z
CC       ring septums. Rapidly oscillates between the poles of the cell to
CC       destabilize FtsZ filaments that have formed before they mature into
CC       polar Z rings. Prevents FtsZ polymerization. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
CC   -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
CC   -!- SIMILARITY: Belongs to the MinC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
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DR   EMBL; CP000026; AAV77030.1; -; Genomic_DNA.
DR   RefSeq; WP_000072527.1; NC_006511.1.
DR   AlphaFoldDB; Q5PI83; -.
DR   SMR; Q5PI83; -.
DR   DNASU; 3177565; -.
DR   EnsemblBacteria; AAV77030; AAV77030; SPA1059.
DR   KEGG; spt:SPA1059; -.
DR   HOGENOM; CLU_067812_0_1_6; -.
DR   OMA; RRDPLWG; -.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0051302; P:regulation of cell division; IEA:InterPro.
DR   GO; GO:1901891; P:regulation of cell septum assembly; IEA:InterPro.
DR   Gene3D; 2.160.20.70; -; 1.
DR   HAMAP; MF_00267; MinC; 1.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR013033; MinC.
DR   InterPro; IPR036145; MinC_C_sf.
DR   InterPro; IPR007874; MinC_N.
DR   InterPro; IPR005526; Septum_form_inhib_MinC_C.
DR   PANTHER; PTHR34108; PTHR34108; 1.
DR   Pfam; PF03775; MinC_C; 1.
DR   Pfam; PF05209; MinC_N; 1.
DR   SUPFAM; SSF63848; SSF63848; 1.
DR   TIGRFAMs; TIGR01222; minC; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Septation.
FT   CHAIN           1..235
FT                   /note="Probable septum site-determining protein MinC"
FT                   /id="PRO_1000047853"
FT   REGION          104..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   235 AA;  25246 MW;  FF4165927F34056A CRC64;
     MSNTPIELKG SSFTLSVVHL HEAEPEVIRQ ALEDKIAQAP AFLKHAPVVI NVSGLESPVN
     WPELHKIVTS TGLRIIGVSG CKDASLKVEI DRMGLPLLTE GKEKAVRPAP VEPATPSEPP
     QNANPITKTR LIDVPVRSGQ RIYAPQCDLI VTSHVSAGAE LIADGNIHVY GMMRGRALAG
     ASGDREAQIF CTHLTAELVS IAGVYWLSDK IPAEFYGKAA RLRLADNALT VQPLN