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
//