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Database: UniProt
Entry: H6WW37_STREE
LinkDB: H6WW37_STREE
Original site: H6WW37_STREE 
ID   H6WW37_STREE            Unreviewed;      1856 AA.
AC   H6WW37;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Zinc metalloprotease C {ECO:0000313|EMBL:AFB77164.1};
DE            EC=3.4.21.74 {ECO:0000313|EMBL:AFB77164.1};
GN   Name=zmpC {ECO:0000313|EMBL:AFB77164.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:AFB77164.1};
RN   [1] {ECO:0000313|EMBL:AFB77164.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Menon B.B., Gipson I.K.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M26 family.
CC       {ECO:0000256|ARBA:ARBA00005425}.
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DR   EMBL; JQ320497; AFB77164.1; -; Genomic_DNA.
DR   RefSeq; WP_001810309.1; NZ_WNHO01000019.1.
DR   MEROPS; M26.003; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.110; -; 1.
DR   Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR011493; GLUG.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR011505; Peptidase_M26_C_dom.
DR   InterPro; IPR008006; Peptidase_M26_N_dom.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   NCBIfam; TIGR01168; YSIRK_signal; 1.
DR   Pfam; PF07501; G5; 1.
DR   Pfam; PF07581; Glug; 1.
DR   Pfam; PF07580; Peptidase_M26_C; 1.
DR   Pfam; PF05342; Peptidase_M26_N; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   SMART; SM01208; G5; 1.
DR   PROSITE; PS51109; G5; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Hydrolase {ECO:0000313|EMBL:AFB77164.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:AFB77164.1};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AFB77164.1};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        101..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          228..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1856 AA;  206764 MW;  E494D35EF0AA45A5 CRC64;
     MSRKSIGEKR HSFSMRKLSV GLVSVTVSSF FLMSQGIQSV SADNMESPIH YKYMTEGKLT
     DEEKSLLVEA LPQLAEESDD TYYLVYRSQQ FLPNTGFNPT VGTFLFTAGL SLLVLLVSKR
     ENGKKRLVHF LLLTSMGVQL LPASAFGLTS QILSAYNSQL SIGVGEHLPE PLKIEGYQYI
     GYIKTKKQDN TELSRTVDGK YSAQRDSQPN STKTSDVVHS ADLEWNQGQG KVSLQGEASG
     DDGLSEKSSI AADNLSSNDS FASQVEQNPD HKGESVVRPT VPEQGNPVSA TTVQSAEEEV
     LATTNDRPEY KLPLETKGTQ EPGHEGEAAV REDLPVYTKP LETKGTQGPG HEGEAAVREE
     EPAYTEPLAT KGTQEPGHEG KATVREETLE YTEPVATKGT QEPEHEGEAA VEEELPALEV
     TTRNRTEIQN IPYTTEEIQD PTLLKNRRKI ERQGQAGTRT IQYEDYIVNG NVVETKEVSR
     TEVAPVNEVV KVGTLVKVKP TVEITNLTKV ENKKSITVSY NLIDTTSAYV SAKTQVFHGD
     KLVKEVDIEN PAKEQVISGL DYYTPYTVKT HLTYNLGENN EENTETSTQD FQLEYKKIEI
     KDIDSVELYG KENDRYRRYL SLSEAPTDTA KYFVKVKSDR FKEMYLPVKS ITENTDGTYK
     VTVAVDQLVE EGTDGYKDDY TFTVAKSKAE QPGVYTSFKQ LVTAMQSNLS GVYTLASDMT
     ADEVSLGDKQ TSYLTGAFTG SLIGSDGTKS YAIYDLKKPL FDTLNGATVR DLDIKTVSAD
     SKENVAALAK AANSANINNV AVEGKISGAK SVAGLVASAT NTVIENSSFT GKLIANHQDS
     NKNDTGGIVG NITGNSSRVN KVRVDALIST NARNNNQTAG GIVGRLENGA LISNSVATGE
     IRNGQGYSRV GGIVGSTWQN GRVNNVVSNV DVGDGYVITG DQYAAADVKN ASTSVDNRKA
     DRFATKLSKD QIDAKVADYG ITVTLDDTGQ DLKRNLREVD YTRLNKAEAE RKVAYSNIEK
     LMPFYNKDLV VHYGNKVATT DKLYTTELLD VVPMKDDEVV TDINNKKNSI NKVMLHFKDN
     TVEYLDVTFK ENFINSQVIE YNVTGKEYIF TPEAFVSDYT AITNNVLSDL QNVTLNSEAT
     KKVLGAANDA ALDNLYLDRQ FEEVKANIAE HLRKVLAMDK SINTTGDGVV EYVSEKIKNN
     KEAFMLGLTY MNRWYDINYG KMNTKDLSTY KFDFNGNNET STLDTIVALG NSGLDNLRAS
     NTVGLYANKL ASVKGEDSVF DFVEAYRKLF LPNKTNNEWF KENTKAYIVE MKSDIAEVRE
     KQESPTADRK YSLGVYDRIS APSWGHKSML LPLLTLPEES VYISSNMSTL AFGSYERYRD
     SVDGVILSGD ALRTYVRNRV DIAAKRHRDH YDIWYNLLDS ASKEKLFRSV IVYDGFNVKD
     ETGRTYWARL TDKNIGSIKE FFGPVGKWYE YNSSAGAYAN GSLTHFVLDR LLDAYGTSVY
     THEMVHNSDS AIYFEGNGRR EGLGAELYAL GLLQSVDSVN SHILALNTLY KAEKDDLNRL
     HTYNPVERFD SDEALQSYMH GSYDVMYTLD AMEAKAILAQ NNDVKKKWFR KIENYYVRDT
     RHNKDTHAGN KVRPLTDEEV ANLTSLNSLI DNDIINRRSY DDNREYKRNG YYTISMFSPV
     YAALSNSKGA PGDIMFRKIA YELLAEKGYH KGFLPYVSNQ YGAEAFASGS KTFSSWHGRD
     VALVTDDLVF KKVFNGEYSS WADFKKAMFK QRIDKQDNLK PITIQYELGN PNSTKEVTIT
     TAAQMQQLIN EAAAKDITNI DRATSHTPAS WVHLLKQKIY NAYLRTTDDF RNSIYK
//
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