ID B2IMX6_STRPS Unreviewed; 1980 AA.
AC B2IMX6;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Zinc metalloprotease ZmpB, putative {ECO:0000313|EMBL:ACB89872.1};
GN Name=zmpB {ECO:0000313|EMBL:ACB89872.1};
GN OrderedLocusNames=SPCG_0620 {ECO:0000313|EMBL:ACB89872.1};
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB89872.1, ECO:0000313|Proteomes:UP000001682};
RN [1] {ECO:0000313|EMBL:ACB89872.1, ECO:0000313|Proteomes:UP000001682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14 {ECO:0000313|EMBL:ACB89872.1,
RC ECO:0000313|Proteomes:UP000001682};
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(2009).
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; CP001033; ACB89872.1; -; Genomic_DNA.
DR RefSeq; WP_000472965.1; NC_010582.1.
DR KEGG; spw:SPCG_0620; -.
DR HOGENOM; CLU_000802_0_0_9; -.
DR Proteomes; UP000001682; Chromosome.
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; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR011505; Peptidase_M26_C_dom.
DR InterPro; IPR008006; Peptidase_M26_N_dom.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR48193:SF2; ZINC METALLOPROTEASE ZMPB; 1.
DR PANTHER; PTHR48193; ZINC METALLOPROTEASE ZMPB-RELATED; 1.
DR Pfam; PF07554; FIVAR; 3.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF07580; Peptidase_M26_C; 1.
DR Pfam; PF05342; Peptidase_M26_N; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049, ECO:0000313|EMBL:ACB89872.1};
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:ACB89872.1};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ACB89872.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1980
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002778878"
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..108
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 172..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 488..548
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 177..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1980 AA; 221380 MW; 91AC88242631C7A8 CRC64;
MFKKDRFSIR KIKGVVGSVF LGSLLMAPSV VDAATYHYVN KEIISQEAKD LIQTGKPDRN
EVVYGLVYQK DQLPQTGTEA SVLTAFGLLT VGSLLLIYKR KKIASVFLVG AMGLVVLPSA
EAVDPVATLA LASREGVVEM DGYRYVGYLS GDILKTLGLD TVLEETSAKP GEVTVVEVET
PQSTTNQEQA RTENQVVETE EAPKEEAPKT EESPKEEPKS EVKPTDDTLP KVEEGKEDSA
EPAPVEEVGG EVESKSEEKV AVKPESQPSD KPAEESKVEQ AGEPVAPRED EKAPVEPEKQ
PEAPEEEKAV EETPKQEDTQ PEVVETKDEA ANQPVEEPKV ETPAVEKQTE PTEEPKVEQV
GEPVEPREDE KAPVSPEKQP EAPEEEKTAE ETPKQEDKIK GIGTKEPVDK SELNNQIDKA
SSVSPTDYST ASYNALGPVL ETAKGVYASE PVKQPEVNSE TKAEKVAANT DAKQSEVNSE
TASLKTAISG LNTDKVELEN QLKIAQGKTE TDFSMESWTV LSTAKNKAQE VKDNGTATQE
QINEAEKSLK TALADLSVDK TALGSAIDTA TKKNKENYTN QTWAELETVL TAAKSVNTNE
SKQSEVNEAV EKLTATIEKL VELSEKPRLT LSIEKRDIDR KVTVTYTLEN PANTQIKSIT
ATLKKGEEVV KDFVLTEENL KTNHLTALFE KLDYYKEYTL STDMVYNRGN DDETESISEE
LIQLNLKKLE LKDIQTVSLM KFENGQESQV THLSDKPTDL SKLYLKVTSS TSKDAVLAVS
SIEEEIVENK KIFKIHADTP ELVVRKKDGS LSKGFDYYME RVIPHDGDIY YDFKDLISAM
TSNPTGTFIL GRDISSRNVK PDGNGKSYIK GEFKGKLLGT NDNVRHSIFD LEYPLFDTIK
SGVVKDIDFK HVNMVFPDSN QGDNVATIAR VIKDKTKIEN VNVEGYLEGR DHVAGLVNNL
EGNSEIENIS FTGKIKSKGG NSITAGIAGR NILSRVKRAY VNANIEVLGS TNSSMLVAVN
GTTLNASGGW GAWGRLTESV AKGTLEIKRS GQAGGVTATV WPYGAIDKVV SYAKVTKGKE
LFGSDGDLNN NWFMQKINNI FGVQGISSGD SGNDSKFKRI SEEEAKQKVA SYNITAPNLM
SDSSLLVDRL NESWKNTDQF ESIQDYQSQN QLIYQNLTKF TPYYNKEFIV HEGNALTPEQ
EILKTKKIKS IVGLKGTEFV VDGSDIDTIM LHFEDGSQKR YKVTSTGKFS ITNLPEYQVE
DLNVVYTSEH IVHPLDSSLI NNLVEELKKV ELYTESTYQV LGIDKDNANK LNRTKRLFLD
ESLDAVKTQL PTFVKTMFEN EWLHINGESS GAVAALRQKI MDNKTAILLA LTYINRYYDV
KFSDYNIKKL MLFKPTFHGE KIDLLDRLIR LGSSGENRLK GSENAETFKQ LFASETKQKD
LVTYLDYNRS LLTNYQTTGE WFKETTKDYI QFEERPSLVE EIKDAKYRVY DNLTAPYYQG
YILPLLTLKN THLAILSNYS TMTFVSREKR PNWKNEDFDK WVKYVATAHR NHVDTWYKIL
PDNIKGKMVK ENVTAVWEGL SIPGSEWVDQ NAVDRKGRDY APAREFFNLV GGPMGGWYAY
HGYGAHAGGR NRVNYEVFDV LSEYGISVFT HELTHVNDTW IYLGGYGRRE NMGPEAYAQG
LFQSPVPGQP GWGALGLNMA FERKNDGDLI YNASPTQFEN RKELDSYMKN YNDTLMMVDY
LEGDAVISKG KEAITKWFKK VEPKVVSQTA QYDTVRQLTA EEKEKLSVSS VDDLVDQGLM
SDRAVGNNTY NPADFETSYI AIDYMTGIYG GGKNSVGSPG ALMFKHNTFR MWGYYGFEEG
VLGYASNKFK QASRDEGHAG LSDNFIISKI SKGEFLTMEA FKKGYFKKVV EELKTKGIRP
VTINQKTYST FEELQEGFKQ AVERDLKKNQ LDERETRNFK FQVFRQLLQQ TDSFKTSIFR
//
