#=GF ID Mobilization_B
#=GF AC PF17511.6
#=GF DE Mobilization protein B
#=GF AU El-Gebali S;0000-0003-1378-5495
#=GF SE PRODOM:PD078829
#=GF GA 27.00 27.00;
#=GF TC 27.80 27.80;
#=GF NC 26.90 26.90;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Family
#=GF RN [1]
#=GF RM 19465049
#=GF RT Replication and conjugative mobilization of broad host-range
#=GF RT IncQ plasmids.
#=GF RA Meyer R;
#=GF RL Plasmid. 2009;62:57-70.
#=GF RN [2]
#=GF RM 21622757
#=GF RT Functional organization of MobB, a small protein required for
#=GF RT efficient conjugal transfer of plasmid R1162.
#=GF RA Meyer R;
#=GF RL J Bacteriol. 2011;193:3904-3911.
#=GF DR INTERPRO; IPR020369;
#=GF DR SO; 0100021; polypeptide_conserved_region;
#=GF CC This is a family of unknown function found in Bacteria. Family
#=GF CC members include Mobilization protein B (MobB). MobB contains a
#=GF CC putative membrane-spanning domain, and might be involved in
#=GF CC anchoring or presenting MobA, and the covalently-linked plasmid
#=GF CC DNA, to the conjugative pore for subsequent export. In agreement
#=GF CC with this, MobB has been shown to be associated with the
#=GF CC membrane. Deletion of the membrane-spanning domain disrupts this
#=GF CC association and decreases the frequency of both type IV
#=GF CC transport and plasmid mobilization. MobB is one out of three
#=GF CC proteins encoded by RSF1010 that are required for its
#=GF CC mobilization along with MobA and MobC [1]. MobB encoded by the
#=GF CC broad-host-range plasmid R1162 is required for its efficient
#=GF CC transfer by conjugation. The C-terminal half of the protein
#=GF CC contains a membrane domain essential for transfer, while the
#=GF CC other, functionally active region of MobB, identified by
#=GF CC mutagenesis, is at the N-terminal end. One mutation affecting
#=GF CC this region inhibits replication, suggesting that this part of
#=GF CC the protein is contacting and sequestering the relaxase-linked
#=GF CC primase. A model that represents MobB molecules as anchored in
#=GF CC the membrane at one end and engaging the relaxase at the other.
#=GF CC This arrangement is suggested to increase the transfer frequency
#=GF CC by raising the probability of contact between the relaxase and
#=GF CC the membrane-embedded, coupling protein for type IV secretion
#=GF CC [2].
#=GF SQ 6
#=GS A0A562R8L6_9BURK/24-151 AC A0A562R8L6.1
#=GS G2J978_9BURK/24-133 AC G2J978.1
#=GS A0A7H9BNT5_9NEIS/23-149 AC A0A7H9BNT5.1
#=GS A0A1H8MRM2_9BURK/25-138 AC A0A1H8MRM2.1
#=GS A0A7Y6NTE7_9BURK/24-142 AC A0A7Y6NTE7.1
#=GS A0A848FL41_9BURK/22-143 AC A0A848FL41.1
A0A562R8L6_9BURK/24-151 qgiealhsarie--------..---NVEQLASMLEPLAQAMAALTDET...RQTLTEIEQQGRDQAERFKSQVEAATKALTQASTQ-------AQQAASNMDAAARQTEWRHYLLVVITGLLSGL-L.VSALWLWQARYALEAEPS--------ikgaavv................
G2J978_9BURK/24-133 gqmetlrqtehq--------..---NAQALAATLEPLAQAMAALTDET...RQTLTEIDSKSREQIETFKQQIGNSARAWNNAAAEAKRAADSLNQAGQR--MEWRHYALAALTGAVTAVLIHIL--.--------------------------gvk....................
A0A7H9BNT5_9NEIS/23-149 ..........as--QIETVRqaKHQSAEDLAATLEPLAQAMAALADET...RQTLAEIDRKSREQGETFTRQLSESVKGY-------KDAVAAASQAAESLNQAGQRMEWRHYGLAVV-TGLVTAAL.VSGFWLWLAPPKV-------------qnmldaqava.............
A0A1H8MRM2_9BURK/25-138 ....qieslrea--------..KLSSVDELASLLEPLAKAMAVLTQETlssVRKIEQIEQRSRDQNTQFKIQMEGALTSWKQAVLEAEAAVSKMGRLGEN--SAVRT--------------------.--------------------------vltavltglftgllstaswllla
A0A7Y6NTE7_9BURK/24-142 ....qqvqavsn-------A..KSQSAEELAATLEPLAQALAALSAET...AKTLAEIDSRTRATGASFTLQLET-------ATKTLNAATVQAQRATVGLHQAAKRLDWTHYALTVTTAL--LTAVlVSGFWLWLRPPTV-------------qtf....................
A0A848FL41_9BURK/22-143 ....lsgqieql-----RQA..KHQSVEELAAALEPLAQAMAALADET...KTTLAEIQQKAREQGEKFTGQMNEAAKSWNQAAEHAAQAGTRLELAGQR--LEWRHYALAGMTGLLTAALVS----.--VFWLWVAP----------------ptspeit................
#=GC seq_cons ....t.tphcpp..........K.pSsE-LAAsLEPLAQAMAALoDET...+pTLsEI-p+oR-QuEpFptQlpsus+uappAstphptAssphppAups..tAsR+hthtthshsVsssLl.hh.....shWLW.t..................st..h.................
//
