COMA_STRR6
ID COMA_STRR6 Reviewed; 717 AA.
AC P59653;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transport/processing ATP-binding protein ComA;
DE EC=3.4.22.-;
DE EC=7.4.2.-;
GN Name=comA; OrderedLocusNames=spr0043;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
CC -!- FUNCTION: Required for induction of competence. Seems to transport the
CC competence-stimulating peptide (CSP) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. HlyB family.
CC {ECO:0000305}.
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DR EMBL; AE007317; AAK98847.1; -; Genomic_DNA.
DR RefSeq; NP_357637.1; NC_003098.1.
DR RefSeq; WP_000668290.1; NC_003098.1.
DR AlphaFoldDB; P59653; -.
DR SMR; P59653; -.
DR STRING; 171101.spr0043; -.
DR MEROPS; C39.001; -.
DR EnsemblBacteria; AAK98847; AAK98847; spr0043.
DR GeneID; 60234023; -.
DR KEGG; spr:spr0043; -.
DR PATRIC; fig|171101.6.peg.51; -.
DR eggNOG; COG2274; Bacteria.
DR HOGENOM; CLU_000604_84_3_9; -.
DR OMA; QQSHFIE; -.
DR Proteomes; UP000000586; 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:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
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 GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; Reference proteome; Thiol protease;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..717
FT /note="Transport/processing ATP-binding protein ComA"
FT /id="PRO_0000092235"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
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 281..301
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"
SQ SEQUENCE 717 AA; 80350 MW; 54FDD6EEE0DBD59E CRC64;
MKFGKRHYRP QVDQMDCGVA SLAMVFGYYG SYYFLAHLRE LAKTTMDGTT ALGLVKVAEE
IGFETRAIKA DMTLFDLPDL TFPFVAHVLK EGKLLHYYVV TGQDKDSIHI ADPDPGVKLT
KLPRERFEEE WTGVTLFMAP SPDYKPHKEQ KNGLLSFIPI LVKQRGLIAN IVLATLLVTV
INIVGSYYLQ SIIDTYVPDQ MRSTLGIISI GLVIVYILQQ 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
ISLGGVNLNQ IDKKALRQYI NYLPQQPYVF NGTILENLLL GAKEGTTQED ILRAVELAEI
REDIERMPLN YQTELTSDGA GISGGQRQRI ALARALLTDA PVLILDEATS SLDILTEKRI
VDNLIALDKT LIFIAHRLTI AERTEKVVVL DQGKIVEEGK HADLLAQGGF YAHLVNS
