COMA_STRPN
ID COMA_STRPN Reviewed; 717 AA.
AC Q03727;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Transport/processing ATP-binding protein ComA;
DE EC=3.4.22.-;
DE EC=7.4.2.-;
GN Name=comA; OrderedLocusNames=SP_0042;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rx / CP1200;
RX PubMed=1987129; DOI=10.1128/jb.173.1.372-381.1991;
RA Hui F.M., Morrison D.A.;
RT "Genetic transformation in Streptococcus pneumoniae: nucleotide sequence
RT analysis shows comA, a gene required for competence induction, to be a
RT member of the bacterial ATP-dependent transport protein family.";
RL J. Bacteriol. 173:372-381(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 713-717.
RC STRAIN=Rx / CP1200;
RX PubMed=7883181; DOI=10.1016/0378-1119(94)00841-f;
RA Hui F.M., Zhou L., Morrison D.A.;
RT "Competence for genetic transformation in Streptococcus pneumoniae:
RT organization of a regulatory locus with homology to two lactococcin A
RT secretion genes.";
RL Gene 153:25-31(1995).
CC -!- FUNCTION: Required for induction of competence. Seems to transport the
CC competence-stimulating peptide (CSP).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Competence
CC factor exporter (TC 3.A.1.112.1) family. {ECO:0000305}.
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DR EMBL; M36180; AAA69510.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74231.1; -; Genomic_DNA.
DR PIR; A39203; A39203.
DR PIR; C97877; C97877.
DR PIR; F95004; F95004.
DR RefSeq; WP_000668284.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q03727; -.
DR SMR; Q03727; -.
DR STRING; 170187.SP_0042; -.
DR MEROPS; C39.001; -.
DR TCDB; 3.A.1.112.1; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAK74231; AAK74231; SP_0042.
DR KEGG; spn:SP_0042; -.
DR eggNOG; COG2274; Bacteria.
DR OMA; QQSHFIE; -.
DR PhylomeDB; Q03727; -.
DR BioCyc; SPNE170187:G1FZB-47-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043214; F:ABC-type bacteriocin transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005897; Pept_C39_ABC_bacteriocin.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR01193; bacteriocin_ABC; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Competence; Hydrolase; Membrane;
KW Nucleotide-binding; Protease; Thiol protease; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..717
FT /note="Transport/processing ATP-binding protein ComA"
FT /id="PRO_0000092234"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 11..138
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 168..450
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 484..717
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT BINDING 517..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 218
FT /note="F -> L (in Ref. 1; AAA69510)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="S -> G (in Ref. 1; AAA69510)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="S -> P (in Ref. 1; AAA69510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 80404 MW; 06A51085A902F608 CRC64;
MKFGKRHYRP QVDQMDCGVA SLAMVFGYYG SYYFLAHLRE LAKTTMDGTT ALGLVKVAEE
IGFETRAIKA DMTLFDLPDL TFPFVAHVLK EGKLLHYYVV TGQDKDSIHI ADPDPGVKLT
KLPRERFEEE WTGVTLFMAP SPDYKPHKEQ KNGLLSFIPI LVKQRGLIAN IVLATLLVTV
INIVGSYYLQ SIIDTYVPDQ MRSTLGIISI GLVIVYIFQQ ILSYAQEYLL LVLGQRLSID
VILSYIKHVF HLPMSFFATR RTGEIVSRFT DANSIIDALA STILSIFLDV STVVIISLVL
FSQNTNLFFM TLLALPIYTV IIFAFMKPFE KMNRDTMEAN AVLSSSIIED INGIETIKSL
TSESQRYQKI DKEFVDYLKK SFTYSRAESQ QKALKKVAHL LLNVGILWMG AVLVMDGKMS
LGQLITYNTL LVYFTNPLEN IINLQTKLQT AQVANNRLNE VYLVASEFEE KKTVEDLSLM
KGDMTFKQVH YKYGYGRDVL SDINLTVPQG SKVAFVGISG SGKTTLAKMM VNFYDPSQGE
ISLGSVNLNQ IDKKALRQYI NYLSQQPYVF NGTILENLLL GAKEGTTQED ILRAVELAEI
REDIERMPLN YQTELTSDGA GISGGQRQRI ALARALLTDA PVLILDEATS SLDILTEKRI
VDNLIALDKT LIFIAHRLTI AERTEKVVVL DQGKIVEEGK HADLLAQGGF YAHLVNS
