ID   ZMPB_STRR6              Reviewed;        1876 AA.
AC   Q8DQN5;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Zinc metalloprotease ZmpB;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=zmpB; OrderedLocusNames=spr0581;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Secreted,
CC       cell wall {ECO:0000250}; Peptidoglycan-anchor {ECO:0000250}.
CC   -!- PTM: The Gram-positive cell-wall anchor motif LPXTG is located in the
CC       N-terminal part, in contrast to such motifs in other known
CC       streptococcal and staphylococcal proteins. The protease could be
CC       cleaved by the sortase and anchored in the membrane via the two
CC       potential N-terminal transmembrane domains, whereas the propeptide
CC       located prior to the LPXTG motif would remain attached to the cell wall
CC       peptidoglycan by an amide bond (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M26 family. {ECO:0000305}.
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DR   EMBL; AE007317; AAK99385.1; -; Genomic_DNA.
DR   PIR; E97944; E97944.
DR   RefSeq; NP_358175.1; NC_003098.1.
DR   RefSeq; WP_000473008.1; NC_003098.1.
DR   AlphaFoldDB; Q8DQN5; -.
DR   SMR; Q8DQN5; -.
DR   STRING; 171101.spr0581; -.
DR   PRIDE; Q8DQN5; -.
DR   EnsemblBacteria; AAK99385; AAK99385; spr0581.
DR   GeneID; 60232697; -.
DR   KEGG; spr:spr0581; -.
DR   PATRIC; fig|171101.6.peg.648; -.
DR   eggNOG; COG3064; Bacteria.
DR   HOGENOM; CLU_000802_0_0_9; -.
DR   OMA; TQEVGHE; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR011505; Peptidase_M26_C_dom.
DR   InterPro; IPR008006; Peptidase_M26_N_dom.
DR   Pfam; PF07501; G5; 2.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF07580; Peptidase_M26_C; 1.
DR   Pfam; PF05342; Peptidase_M26_N; 1.
DR   SMART; SM01208; G5; 2.
DR   PROSITE; PS51109; G5; 2.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Peptidoglycan-anchor; Protease; Reference proteome; Repeat; Secreted;
KW   Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   PROPEP          34..76
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026843"
FT   CHAIN           77..1876
FT                   /note="Zinc metalloprotease ZmpB"
FT                   /id="PRO_0000026844"
FT   TRANSMEM        77..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..1876
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          359..434
FT                   /note="G5 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT   DOMAIN          435..516
FT                   /note="G5 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT   REGION          172..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           73..77
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        177..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1530
FT                   /evidence="ECO:0000250"
FT   BINDING         1529
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1533
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1553
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         76
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1876 AA;  211058 MW;  E7E93FA7A103A5B2 CRC64;
     MFKKDRFSIR KIKGVVGSVF LGSLLMAPSV VDAATYHYVN KEIISQEAKD LIQTGKPDRN
     EVVYGLVYQK DQLPQTGTEA SVLTAFGLLT VGSLLLIYKR KKIASVFLVG TMGLVVLPSA
     GAVDPVATLA LASREGVVEM EGYRYVGYLS GDILKTLGLD TVLEETSAKP GEVTVVEVET
     PQSTTNQEQA RTENQVVETE EAPKEEAPKT EESPKEEPKS EVKPTDDTLP KVEEGKEDSA
     EPAPVEEVGG EVESKPEEKV AVKPESQPSD KPAEESKVEQ AGEPVAPRKD EQAPVEPENQ
     PEAPEEEKAV EETPKQEEST PDTKAEETVE PKEETKTAKG TQEEGKEGQA PVQEVNPEYK
     VTTGTVEKST ESELDFTTEV VPDDTKYVDE EVVERQGSKG VQVTKTTYET VEVVETDKVL
     STTTEVKTPV VPKVVKKGTK PVETREEVIP FATKEQEDDT LKRGTRQVAQ EGVNGKKQIT
     ETYKTIRGEK TNEAPTVEET VLQAPQDEII KKGTKGLEKP TLQWANTEKD VLKKSATASY
     TLTKPAGVEI KSIKLALKDK DGQLVKEVTV AENNLNATLD KLKYYQGYTL STTMVYDRGE
     GEETEKLEDK QIQLDLKKVE IKNIKETSLM NVDAEGNETD KSLLSEKPTD VSQLYLRVTT
     HDNKVTRLAV SSVEEVVVDG KTLYKVVAKA PDLVQRRADD TLSEEYVHYF EKQLPKVNNV
     YYNFNELVKD MQANPMGEFK LGADLNAVNV KPAGKAYVMA KFRGTLSSVE NHQYTIHNLE
     RPLFNEAEGA TLKNFNLGNV NINMPWADKV APIGNMFKKS TLENIKVVGS VTGNNDVTGA
     VNKLDEANMR NVAFIGKINS LGDKGWWSGG LVSESWRSNT DSVYFDGDIV GNNSKFGGLV
     AKVNHGSNQW DVKQKGRLTN SVVKGTMTLK NHGQSGGLVH ENYDWGWVEN NISMMKVNNG
     EIMYGSGSID GDPYFGFDYF KNNYYVKDVA TGESTYKRSK QIQSISQAEA DAKIANMGIT
     ANTFAIQDPV VNKLNRIIDR DSEYKAIQDY QETRNLAYRN LEKLQPFYNK EWIVNQGNKL
     TDESNLVKKT VLSVTGMKSG QFVTDLSSVD KIMIHYADGT KEEFGVSAIS DSRVKQVKEY
     NVDDLGVVYT PNMVDKNRDS LITKVKEKLS SVALDSAEVK SITNNPASLY LEESFAEVRE
     TLDKLVKSLL ENEDHQLNSD EVAEKALLKK VEDNKAKIIL ALTYLNRYYG IDYDGLNFKH
     LMMFKPDFYG KTPSILDFLI RIGSAEKNLK GDRSLEAYRE VIGGTIGKGE LNGLLGYNMR
     LFTKYTDLND WFIHAAKNVY VSEPETTTED FKDKRHRIYD GLNNDVHGRM ILPLLNLKKA
     HIFVISTYNT IAFSSFEKYG KNTEEERNAY KAEIDRVAKA QQRYLDFWSR LALPKVRNQL
     LKSQNSVPTP VWDNQVYVGL GGANRMGYGD GGRVVTPVRE LFGPTDRWHQ INWNMGAMAK
     IYERPWKDDQ VYFMVTNMME PFGISAFTHE TTHVNDRMAY YGGDWHREGT DLEAFAQGML
     QTPDKSTTNG EYGALGINMA YERKNDGEQL YNYDPEKLDS REKIDSYMKN YNESMMMLDY
     LEASAVIRQN LSDNSKWFKK MDKEWRTNAD RNRLIGEPHQ WDKLRDLTEE EKKLPIDSID
     KLVENNFVTL HGMPKNGRYR TEGFDSSYQP VNMMAGVFGG NTSKSTVGSI SFKHNAFRMW
     GYYGYENGFI PYVSNKLKGA ANKENKGLLG DDFIIKKVSK NQFQNLEEWK KHWYHEVYDK
     AQKGFVEIEV DGVKISTYAQ LQSLFEEAVS KDLAGMDDKN IKNHYQYTEN LKWKIYKQLL
     KNTDGFSSDL FTAPQA